LOCUS       BAA84474                3972 aa            linear   BCT 18-SEP-1999
DEFINITION  type I polyketide synthase AVES 1 [Streptomyces avermitilis].
ACCESSION   BAA84474
VERSION     BAA84474.1
DBSOURCE    accession AB032367.1
KEYWORDS    .
SOURCE      Streptomyces avermitilis
  ORGANISM  Streptomyces avermitilis
            Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
            Streptomyces.
REFERENCE   1  (residues 1 to 3972)
  AUTHORS   Ikeda,H., Nonomiya,T., Usami,M., Ohta,T. and Omura,S.
  TITLE     Organization of the biosynthetic gene cluster for the polyketide
            anthelmintic macrolide avermectin in Streptomyces avermitilis
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 96 (17), 9509-9514 (1999)
   PUBMED   10449723
REFERENCE   2  (residues 1 to 3972)
  AUTHORS   Ikeda,H., Nonomiya,T., Usami,M., Ohta,T. and Omura,S.
  TITLE     Direct Submission
  JOURNAL   Submitted (13-SEP-1999) Haruo Ikeda, School of Pharmaceutical
            Sciences, Kitasato University, Microbial chemistry; 5-9-1
            Shirokane, Minato-ku, Tokyo 108-8641, Japan
            (E-mail:ikeda@mc.pharm.kitasato-u.ac.jp, Tel:+81-3-5791-6242,
            Fax:+81-3-3444-6197)
FEATURES             Location/Qualifiers
     source          1..3972
                     /organism="Streptomyces avermitilis"
                     /db_xref="taxon:33903"
     Protein         1..3972
                     /product="type I polyketide synthase AVES 1"
     Region          <13..>354
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:225858"
     Region          31..336
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          366..453
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          481..909
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Region          483..911
                     /region_name="PKS_KS"
                     /note="Beta-ketoacyl synthase; smart00825"
                     /db_xref="CDD:214836"
     Site            order(657,792,831)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          862..995
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          1052..1349
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          1476..1944
                     /region_name="KR_1_SDR_x"
                     /note="ketoreductase (KR), subgroup 1, complex (x) SDRs;
                     cd08952"
                     /db_xref="CDD:187655"
     Site            order(1747..1750,1775..1778,1802..1804,1825..1826,
                     1848..1849,1863,1890..1891)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187655"
     Site            order(1826,1850,1863,1867)
                     /site_type="active"
                     /db_xref="CDD:187655"
     Region          1979..2064
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          2083..3182
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:225858"
     Region          2086..2510
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Site            order(2258,2393,2433)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          2473..2590
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          2641..2916
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          3005..3176
                     /region_name="PKS_DH"
                     /note="Dehydratase domain in polyketide synthase (PKS)
                     enzymes; smart00826"
                     /db_xref="CDD:214837"
     Region          3312..3763
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(3545..3546,3548,3569..3572,3597..3600,3624..3626,
                     3647..3648,3670..3671,3685,3712..3713)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(3648,3672,3685,3689)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          3805..3890
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     CDS             1..3972
                     /gene="aveA1"
                     /coded_by="AB032367.1:101..12019"
                     /note="contains a loading module, Ave module 1 and module
                     2;
                     multifunctional polyketide synthase"
                     /transl_table=11
ORIGIN      
        1 mqrmdggeep rpaagevlgv adeadggvvf vfpgqgpqwp gmgrelldas dvfresvrac
       61 eaafapyvdw sveqvlrdsp dapgldrvdv vqptlfavmi slaalwrsqg vepcavlghs
      121 lgeiaaahvs gglsladaar vvtlwsqaqt tlagtgalvs vaatpdellp riapwtednp
      181 arlavaavng prstvvsgar eavadlvadl taaqvrtrmi pvdvpahspl myaieervvs
      241 gllpitprps ripfhssvtg grldtrelda aywyrnmsst vrfepaarll lqqgpktfve
      301 msphpvltmg lqelapdlgd ttgtadtvim gtlrrgqgtl dhfltslaql rghgetsatt
      361 vlsarltals ptqqqsllld lvrahtmavl nddgnertas dagpsasfah lgfdsvmgve
      421 lrnrlskatg lrlpvtlifd httpaavaar lrtaalghld edtapvpdsp sghggtaaad
      481 dpiaiigmac rfpggvrspk dlwelaasgg daigpfptdr gwpteqrhaq dptqpgtfyp
      541 qgggflhdaa hfdagffgis prealamdpq qrllletswe aferagidpl svrgsrtgvf
      601 agalsfdygp rmdtassega adveghiltg ttgsvlsgri aysfglegpa itvdtgcsas
      661 lvtlhlacqs lrsgectlal aggvsvmstl gmfiefsrqr glsvdgrcka ysaaadgtgw
      721 gegvgmllve rlsdavrlgh rvlavvrgsa vnqdgasngl tapngpaqer virqalanag
      781 lsvadvdvve ghgtgttlgd pieaqallat ygqragdrpl wlgslksnig htmaaagvgg
      841 vikmvmalre gvlprtlhvd kpspqvdwsa gavrllteav pwpgdaagrl rragvssfgi
      901 ggtnahvile eapaaggcva gggvlegapg laisvaesva apvavsapva esvpvpvpvp
      961 vpvpvsarse aglraqaeal rqyvavrpdv sladvgagla cgravlehra vvlaadreel
     1021 vqglgalaag epdrrvttgh apggdrggvv fvfpgqggqw agmgvrllas spvfarrmqa
     1081 ceealapwvd wsvvdilrrd agdavwerad vvqpvlfsvm vslaalwrsy giepdavlgh
     1141 sqgeiaaahv cgalslkdaa ktvalrsral aavrgrggma svplpaqeve qligerwagr
     1201 lwvaavngpr stavsgdaea vdevlaycag tgvrarripv dyashcphvq plreellell
     1261 gdispqpsgv pffstvegtw ldtttldaay wyrnlhqpvr fsdavqalad dghrvfvevs
     1321 phptlvpaie dttedtaedv taigslrrgd ndtrrfltal ahthttgigt pttwhhhyth
     1381 hhthphphth ldlptypfqh qhywlessqp gagsgsgaga gsgagsgrag taggtaeves
     1441 rfwdavarqd letvattlav ppsagldtvv palsawhrhq hdqarintwt yqetwkpltl
     1501 ptthqphqtw liaipetqth hphitniltn lhhhgitpip ltlnhthtnp qhlhhtlhht
     1561 rqqaqnhttg aitgllslla ldetphphhp htptgtllnl tltqthtqth pptplwyatt
     1621 nattthpndp lthptqaqtw glarttlleh pthtagiidl pttptphtlq hltqtltqph
     1681 hqtqlairtt gthtrrltpt tltpthqppt ptphgttlit ggtgalathl thhltthqpt
     1741 qhllltsrtg phtphaqhlt tqlqqkgihl tittcdtsnp dqlqqllnti ppqhplttvi
     1801 htagilddat ltnltptqln nvlrakahsa hllhqltqht pltafvlyss aaatfgapgq
     1861 anyaaanayl dalahhrhth hlpatsiawg twqgnglads dkarayldrr gfrpmspela
     1921 taavtqaiad terpyvviad idwskiehts qtsdlvsaar erepavqrpt ppaelhktla
     1981 hqtsadqraa llelvrdhva avlrhadpka iapdqsfral gfdsltavef rnllikatgl
     2041 rlpvslvfdh ptpaklavhl qnqlrgtaae sapsaaavta easvtepiai vgmacrfpgg
     2101 vtsaddfwdl isseqdaigg fptdrgwdld tlydpdpdhp gtcytrnggf lydaghfdae
     2161 ffgispreal amdpqqrlll etawetieha ginphtlhgt ptgvftgtng qdyalrvhna
     2221 gqstdgfalt gtagsvisgr isytfgfegp avsvdtacss slvalhlacq alragecsma
     2281 laggvtvmss pgafvefsrq rglaadghck afsaaadgtg wgegvgmllv erlsdahrng
     2341 hrvlavvrgs avnqdgasng ltapngpsqq rvirqalana glsagdvdav eahgtgttlg
     2401 dpieaqalla tygqdrageg plwlgsvksn vghtqaaagv agvikmvmal rhgllprtlh
     2461 vdepsphvdw sagavqllte tvpwpggegr lrragvssfg vsgtnahvil eeapaddvpg
     2521 gppagegdag sddeaaagsp gvwpwlvsak sqpalraqaq alhahltdhp gldladvgyt
     2581 laharavfdh ratliaadrd tflqalqala agephpavih ssapggtgtg eaagktafic
     2641 sgqgtqrpgm ahglyhthpv faaalndict hldphldhpl lplltqndnd nedaaallqq
     2701 tryaqpalfa fqvalhrllt dgyhitphyy aghslgeita ahlagiltlt dattlitqra
     2761 tlmqtmppgt mttlhttphh ithhltahen dlaiaaintp tslvisgtph tvqhittlcq
     2821 qqgiktktlp tnhafhspht npilnqlhqh tqtltyhpph tplitantpp dqlltphywt
     2881 qqarntvdya tttqtlhqhg vttyielgpd ntlttlthhn lpnpptttlt lthphhhpqt
     2941 hlltnlaktt ttwhphhyth hdnqphthth ldlptypfqh hhywlestqp gagnvsaagl
     3001 dptehpllga tlelatdgga llagrlslrs hpwladhavg gtvllsgatf lelalhagty
     3061 vgcdrvdelt lhaplvvpvd ggvsvqvgva aadgegrrlv svyarggsac ggggasggvw
     3121 tchasgvlve aaaggvvvdg lagvwpprga vavdvdgvrd rlagagcvlg pvfsglravw
     3181 rdggdllaev clpeeawgda agfglhpall dgvvqplsvl lpggtgfgeg agfgegvrvp
     3241 avwggvslhr agvtgvrvrv savgrgggre avsvvvgdea gvpvasvdrl elrpvdmgql
     3301 ravsvsagrr gslyavqwae vgpvpvcgqa wawhedvges gggpvpgvvv lrcpdagagg
     3361 gggggggggv gevvggvlgv vqgwlglerf agsrlvvvtr gavvagpedg pvdvvgasvw
     3421 glvrsaqaeh pdrfvlldld tdtgtdldtg agagwgvdgg rvaavvacge pqlavrgerl
     3481 laarlkrles sgdvpaqrsg dtrarrsdvp aqrsggvpar rsvdvsgrev lpwlsggsvl
     3541 vtggtgvlga avarhlagvc gvrdlllvsr rgpdapgaeg lraelaalga evrivacdvg
     3601 errevvrlle gvpagcpltg vvhaagvldd atiasltper lgtvfaakvd aallldeltr
     3661 gmelsafvlf ssaagilgsa gqgnyaaana aldalayrrr aaglpgvsla wglweeasgm
     3721 tghlagtdhr riirsglhpm stpdalalfd aalaldrpvl lpadlrpapp lppllqdllp
     3781 atrrrttrtt ttggadngaq lharlagqth eqqhttllal vrshiatvlg httpdtippd
     3841 rafrdlgfds ltavelrnrl srttglrlpt tlafdhpnpt tlthhlhtql qpqpdnavap
     3901 vlaeldkles alsaldktds aservtlrlk slmlrwnapq hptaesaddd ekftsateae
     3961 ifkfidndlg ls
//

LOCUS       BAA84475                6239 aa            linear   BCT 18-SEP-1999
DEFINITION  type I polyketide synthase AVES 2 [Streptomyces avermitilis].
ACCESSION   BAA84475
VERSION     BAA84475.1
DBSOURCE    accession AB032367.1
KEYWORDS    .
SOURCE      Streptomyces avermitilis
  ORGANISM  Streptomyces avermitilis
            Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
            Streptomyces.
REFERENCE   1  (residues 1 to 6239)
  AUTHORS   Ikeda,H., Nonomiya,T., Usami,M., Ohta,T. and Omura,S.
  TITLE     Organization of the biosynthetic gene cluster for the polyketide
            anthelmintic macrolide avermectin in Streptomyces avermitilis
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 96 (17), 9509-9514 (1999)
   PUBMED   10449723
REFERENCE   2  (residues 1 to 6239)
  AUTHORS   Ikeda,H., Nonomiya,T., Usami,M., Ohta,T. and Omura,S.
  TITLE     Direct Submission
  JOURNAL   Submitted (13-SEP-1999) Haruo Ikeda, School of Pharmaceutical
            Sciences, Kitasato University, Microbial chemistry; 5-9-1
            Shirokane, Minato-ku, Tokyo 108-8641, Japan
            (E-mail:ikeda@mc.pharm.kitasato-u.ac.jp, Tel:+81-3-5791-6242,
            Fax:+81-3-3444-6197)
FEATURES             Location/Qualifiers
     source          1..6239
                     /organism="Streptomyces avermitilis"
                     /db_xref="taxon:33903"
     Protein         1..6239
                     /product="type I polyketide synthase AVES 2"
     Region          5..29
                     /region_name="Docking"
                     /note="Erythronolide synthase docking; pfam08990"
                     /db_xref="CDD:286127"
     Region          33..1105
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:225858"
     Region          36..461
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Site            order(209,344,384)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          424..549
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          600..880
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          978..1063
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1082..2156
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:225858"
     Region          1083..1507
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Site            order(1255,1390,1430)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          1470..1606
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          1657..1937
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          2071..2554
                     /region_name="KR_1_SDR_x"
                     /note="ketoreductase (KR), subgroup 1, complex (x) SDRs;
                     cd08952"
                     /db_xref="CDD:187655"
     Site            order(2338..2341,2366..2369,2393..2395,2416..2417,
                     2439..2440,2454,2481..2482)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187655"
     Site            order(2417,2441,2454,2458)
                     /site_type="active"
                     /db_xref="CDD:187655"
     Region          2577..2660
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          2680..3104
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Region          2682..3106
                     /region_name="PKS_KS"
                     /note="Beta-ketoacyl synthase; smart00825"
                     /db_xref="CDD:214836"
     Site            order(2852,2987,3027)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          3067..3183
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          3234..3511
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          3639..4130
                     /region_name="KR_1_SDR_x"
                     /note="ketoreductase (KR), subgroup 1, complex (x) SDRs;
                     cd08952"
                     /db_xref="CDD:187655"
     Site            order(3910..3913,3938..3941,3965..3967,3988..3989,
                     4012..4013,4027,4054..4055)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187655"
     Site            order(3989,4014,4027,4031)
                     /site_type="active"
                     /db_xref="CDD:187655"
     Region          4159..4244
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          4269..5386
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:225858"
     Region          4271..4698
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Site            order(4445,4580,4620)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          4660..4771
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          4817..5114
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          5189..5362
                     /region_name="PKS_DH"
                     /note="Dehydratase domain in polyketide synthase (PKS)
                     enzymes; smart00826"
                     /db_xref="CDD:214837"
     Region          5505..5994
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(5761..5762,5764,5785..5788,5813..5816,5840..5842,
                     5863..5864,5886..5887,5901,5928..5929)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(5864,5888,5901,5905)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          6032..6117
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     CDS             1..6239
                     /gene="aveA2"
                     /coded_by="AB032367.1:12071..30790"
                     /note="contains Ave module 3, module 4, module 5 and
                     module 6;
                     multifunctional polyketide synthase"
                     /transl_table=11
ORIGIN      
        1 mqlaneakll eylkrvtadl drtrrrlyev vereqepiai vgmacrypgg atsptrlwhl
       61 vksqtdaige fptdrgwnle qlydpdpdrs gtsytrsggf lydagdfdaa ffelspreal
      121 amdpqqrlll ettwetfeqg gidprsmrgs rtgvfvginp edyttgythq psnavegyll
      181 tgsaasiasg risynfgleg paitidtacs sslvalhlac qalrsgectm alaggasvma
      241 tpfvftefsr qrglaadgrc kafsaaadgt gwsegvgmll verlsdarrn ghrvlavvrg
      301 savnqdgasn gltapngrsq vkvirqalan ahlspadvda veahgtgttl gdpieaqalv
      361 eaygqdrpng rplwlgtlks nighsmaaag vggvikmvma lrngllprtl hvdepsphvd
      421 wsagavqllt etvpwpggeg rlrragvssf gvsgtnahvi leeapahnip sdtpaddvpg
      481 esaadedags gdeaaagspg vwpwlvsaks qpalraqaqa lhahltdhpg ldladvgytl
      541 aharavfdhr atliaadrdt flqalqalaa gephpavihs sapggtgtge aagktafics
      601 gqgtqrpgma hglyhthpvf aaalndicth ldphldhpll plltqdpntq dtttleeaaa
      661 llqqtryaqp alfafqvalh rlltdgyhit phyyaghslg eitaahlagi ltltdattli
      721 tqratlmqtm ppgtmttlht tphhithhlt ahendlaiaa intptslvis gtphtvqhit
      781 tlcqqqgikt ktlptnhafh sphtnpilnq lhqhtqtlty hpphtplita ntppdqlltp
      841 hywtqqarnt vdyatttqtl hqhgvttyie lgpdntlttl thdnlpntpt ttltlthphh
      901 hpqthlltnl akttttwhph hythhhnqph ththldlpty pfqhhhywlq ppgkpsdpsp
      961 segreqattp stplrdvlvg kspqerdeel lrlvrthaaa vlghatpevi vpnkafkelg
     1021 fdslaaiqlr nrlladvdlp lpatlifdyp tpmalcqflr aaivgadtgt ttrlpltavp
     1081 adepiaivgm acrypgdvrt vddlwqvvsg ghdaiggfpt nrgwdldtly npdpdhhgts
     1141 ytrsggflyd agnfdpdffg isprealamd pqqrllleta wesiehacin pdslrgtptg
     1201 vfagltyhdy aarfptapag fegylghgsa gsiasgrvay alglegpalt vdtacssslv
     1261 alhlacqalr sgecsmalag gvtvmstpag fvefsrqrgl avdgrckafs aaadgtgwge
     1321 gvgmllverl sdarrlghri lavvrgsavn qdgasnglta pngpsqervi rlalanadlt
     1381 padvdaveah gtgttlgdpi eaqallatyg qdrpgneplw lgsmksnigh aqaaagvggv
     1441 ikmvmalrng llprtlhvde psphvdwsag avqlltetvp wpggegrlrr agvssfgvsg
     1501 tnahvileea pahnipsdtp addapgeaaa ddvpgeaagd dagtggeatg paagspgvwp
     1561 wlvsaksqpa lraqaqalha hltdhpgldl advgytlaha ravfdhratl iaadrdtflq
     1621 alqalaagep hpavihssap ggtgtgeaag ktaficsgqg tqrpgmahgl yhthpvfaaa
     1681 lndicthldp hldhpllpll tqdpntqdtt tleeaaallq qtpyaqpalf afqvalhrll
     1741 tdgyhitphy yaghslgeit aahlagiltl tdattlitqr atlmqtmppg tmttlhttph
     1801 hithhltahe ndlaiaaint ptslvisgtp htvqhittlc qqqgiktktl ptknafhsph
     1861 tnpilnqlhq htqtltyhpp htplitantp pdqlltphyw tqqarntvdy atttqtlhqh
     1921 gvttyielgp dntlttlthh nlpntptttl tlthphhhpq thlltnlakt tttwhphhyt
     1981 hhhnqphtht hldlptypfq hqhywlestq pgagsgsgsg sgragtaggt aevesrfwda
     2041 varqdletva ttlavppsag ldtvvpalsa whrhqhdqar intwtyqetw kpltlptthq
     2101 phqtwliaip etqthhphit niltnlhhhg itpipltlnh thtnpqhlhh trqqaqnhtt
     2161 gpitgllsll aldetphphh phtptgtlln ltltqthtqt hpptplwyat tnattthpnd
     2221 plthptqaqt wglarttlle hpthtagiid lpttptphtl hhltqtltqp hhqtqlairt
     2281 tgthtrrltp ttltpthqpp tptphgttli tggtgalath lthhltthqp tqhllltsrt
     2341 gphtphaqhl ttqlqqkgih ltittcdtsn pdqlqqllnt ippqhplttv ihtagildda
     2401 tltnltptql nnvlrakahs ahllhqltqh tplnafvlys saaatfgapg qanyaaanay
     2461 ldalahhrht hhlpatsiaw gtwqgnglat gqvsehlrrr gmfamppela vtavdgaias
     2521 grpsllvadi dwkklgpvls skssvlledl pqaqgteear stveqtestn lrqllmgrsr
     2581 seqeeellsl vrihsaavlg rddseaippg rlfrdlgfds laavelrnhl aaqtelalpt
     2641 tlvfdypspt klaqfllsei aefqpdnstp lprpraelde piaivgmacr fpggvtsadd
     2701 fwdlisseqd aiggfptdrg wdldtlydpd pdhpgtcytr nggflydagh fdaeffgisp
     2761 realamdpqq rllletawet iehaginpht lhgtptgvft gtngqdhaah irqapsgteg
     2821 fvltgaatsi asgrisyilg legpavtldt acssslvalh lacqslrsge ctmalaggat
     2881 vmttpitfte farqrglapd grckafsaaa dgtgwgegvg mllverlsda rrnghrvlav
     2941 vrgsavnqdg asngltapng psqqrvirqa lanadltpad vdaveahgtg ttlgdpieaq
     3001 ailatygqdr pgngplwlgs vksnvghtqa aagvagvikm vmalrhrtlp ptlhadepsp
     3061 hvdwsagavq lltetvpwpg gegrprragv ssfgvsgtna hvileeapad dvpggppade
     3121 dagsgeeaaa gspgvwpwlv saksqpalra qaqalhahlt dhpgldladv gytlaharav
     3181 fdhratliaa drdtflqalq alaagephpa vihssapggt gtgeaagkta ficsgqgtqr
     3241 pgmahglyht hpvfaaalnd icthldphld hpllplltqn dndndnedaa allqqtpyaq
     3301 palfafqval hrlltdgyhi tphyyaghsl geitaahlag iltltdattl itqratlmqt
     3361 mppgtmttlh ttphhithhl tahendlaia aintptslvi sgtphtvqhi ttlcqqqgik
     3421 tktlptnhaf hsphtnpiln qlhqhtqtlt yhpphtplit antppdqllt phywtqqarn
     3481 tvdyatttqt lhqhgvttyi elgpdntltt lthhnlpntp tttltlthph hhpqthlltn
     3541 lakttttwhp hhythhhnqp hththldlpt ypfqhhhywl elpsaqtspg qrrsrrsapd
     3601 taesefwdav needlqslae tldidasald tvvpalsawh rhqhdqarin twtyqetwkp
     3661 ltlptthqph qtwliaipet qthhphitni ltnlhhhgit pipltvnhth tnpqhlhhtl
     3721 hhtrqqaqnh ttgpitglls llaldetphp hhphtptgtl lnltlpqtht qthpptplwy
     3781 attnattthp ndplthptqa qtwglarttl lehpthtagi idlpttptph tlhhltqtlt
     3841 qphhqtqlai rttgthtrrl tpttltpthq pptptphgtt litggtgala thlthhltth
     3901 qptqhlllts rtgphtphaq hlttqlqqkg ihltittcdt snpdqlqqll ntippqhplt
     3961 tvihtagvnl fapvsetdae sfssvtaaka tgaailhell ldhetlehfi lfssgagawg
     4021 sgnqcaysaa nayldalath rqthglpgas iawgpwagkg msagdaahgy lekrgilpme
     4081 prmalaafhr araqrpnsnl iiadidwerf vpaftarrhs pliedipevr qaaqeleaaa
     4141 staktttaqp iatslrerla rltsskqnqv llglirtgic tvlglrnpeg iedqrafrdl
     4201 gfdsltsaqf skelaketgl plppslvfdy ptpqecaahl rtqlvdldde edaalsnalp
     4261 qvahrrtved epiaiigmac rfpggvrsad dlwellasgk daigvfptdr gwdldtlydp
     4321 dpdhpgtcyt rnggflygag hfdaeffgis prealamdpq qrllletawe tiehaginph
     4381 tlhgtptgvf aginaqdhaa hirqsrdvet iegyaltgss gsvasgrvay tlglegpavs
     4441 vdtacssslv alhwaaqalr agecsmalag gvtvmsspgt fvefsrqrgl aadgrckays
     4501 aaadgtgwae gvgmllverl sdarrnghrv lavvrgsavn qdgasnglta pngpsqqrvi
     4561 rqalanaglt padvdavegh gtgttlgdpi eaqallaayg qhrphhrplw lgslksnigh
     4621 aqaaagvggv ikmvmalrng llpqtlhvde ptpqvdwstg avqlltqpvp wpadpagrpr
     4681 hagvssfgvs gtnahiilee aptpqdsdtd deppanapal phplplpvpv sarseaglra
     4741 qaqalrqyva arpdmspadi gaglargrav lehravilaa dreelaqalt alaagephph
     4801 ittghtrggd rggvvfvfpg qggqwagmgl tlltsspvfa ehidacekal tpwvpwsltd
     4861 ilhrdpddpa wqqadvvqpv lfsimvslaa lwrsygiepd avlghsqgei aaahicgals
     4921 lkdaaktval rsralaavrg rgamaslplp aqdvqqlise rwegqlwvaa lngphsttvs
     4981 gdtkavdevl ahctdtglra kripvdyash cphvqplhde llhllgditp qpstvpffst
     5041 vegtwldttt ldaaywyrnl hqpvrfshai qtltddghra fieisphptl vpaiedtten
     5101 ttenitatgs lrrgdndthr fltalahtht tgigtpttwh hhytqthphp nphthldlpt
     5161 ypfqhqhywl qppttttdlt ttgltpthhp lltatltlad nntqlltgrl slrthpwltd
     5221 htvagmvllp gtallelalq agervdcprv eeltlhaplv iphtedvtlq vtvraadesg
     5281 hralaihsys gtassadrew trhatgllth hadtdhradt htdaclggsw pppgaqpiel
     5341 gdvygrmaad sdiaygpvfq glhaawrfgd dvlaevrlpe ealrdapaaa fgvhpallda
     5401 alhataltpq ngdgstenva qesmpdraah qarlpfswsg vslhtagssv lrvrlsrspq
     5461 hgnavaltaa dedgrpvvti eslalrpvst eelraaadrt peheslfrld wvsvpvpana
     5521 psptadrpwa vigaglphlp gltehehvta ydepadllla ldrgapppgv lvvggvahte
     5581 areysaeapg ergteacear pdvvhvgvvh taavhaaaaq mlarlqawlg derladsrll
     5641 vltcgavara sgddatdlpg aavwglvrsa qsehpdritl ldfergteae pgqlatalnc
     5701 gerqlavrpg glftprlvra prvadavpav pavavpsagh aavpaagpfl pggtvlitgg
     5761 tgvlgrlvar hlveahgvrh lllagrrgpd aegapelrae lgglgatvev vacdaadrqq
     5821 ladlltripd drpltgvvhs agilddgvit slsperlgav lrakadaall ldeltrgael
     5881 safvmfssas avvgspgqgn yaaanavldf lahrrraegl pavslawglw eegtgmtghl
     5941 dvddharisr agmrplptae alalfdaala dgepflmpar ldltavrsga asapvppllq
     6001 gllqlprsrs aaaapghgap aadeaaawre rlarqsager rqallrlvrs hvaavlghsg
     6061 adgidasraf relgfdslta velrnrltaa tglrlratla fdfptpaala ehlgerllpd
     6121 qeatgeqagd qlsggseedv rslltsipig rlrdagllgp lltladtgrg asgaaagped
     6181 appsgqdtpa pvsidemdid dlmdlahghg taparepada edssssrnrt hhthegeta
//

LOCUS       BAA84478                5532 aa            linear   BCT 18-SEP-1999
DEFINITION  type I polyketide synthase AVES 3 [Streptomyces avermitilis].
ACCESSION   BAA84478
VERSION     BAA84478.1
DBSOURCE    accession AB032367.1
KEYWORDS    .
SOURCE      Streptomyces avermitilis
  ORGANISM  Streptomyces avermitilis
            Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
            Streptomyces.
REFERENCE   1  (residues 1 to 5532)
  AUTHORS   Ikeda,H., Nonomiya,T., Usami,M., Ohta,T. and Omura,S.
  TITLE     Organization of the biosynthetic gene cluster for the polyketide
            anthelmintic macrolide avermectin in Streptomyces avermitilis
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 96 (17), 9509-9514 (1999)
   PUBMED   10449723
REFERENCE   2  (residues 1 to 5532)
  AUTHORS   Ikeda,H., Nonomiya,T., Usami,M., Ohta,T. and Omura,S.
  TITLE     Direct Submission
  JOURNAL   Submitted (13-SEP-1999) Haruo Ikeda, School of Pharmaceutical
            Sciences, Kitasato University, Microbial chemistry; 5-9-1
            Shirokane, Minato-ku, Tokyo 108-8641, Japan
            (E-mail:ikeda@mc.pharm.kitasato-u.ac.jp, Tel:+81-3-5791-6242,
            Fax:+81-3-3444-6197)
FEATURES             Location/Qualifiers
     source          1..5532
                     /organism="Streptomyces avermitilis"
                     /db_xref="taxon:33903"
     Protein         1..5532
                     /product="type I polyketide synthase AVES 3"
     Region          35..1154
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:225858"
     Region          38..462
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Site            order(210,345,384)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          415..548
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          605..902
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          976..1148
                     /region_name="PKS_DH"
                     /note="Dehydratase domain in polyketide synthase (PKS)
                     enzymes; smart00826"
                     /db_xref="CDD:214837"
     Region          1352..1714
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(1496..1497,1499,1520..1523,1548..1551,1575..1577,
                     1598..1599,1621..1622,1636,1663..1664)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(1599,1623,1636,1640)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          1756..1841
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1862..2974
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:225858"
     Region          1864..2289
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Site            order(2037,2172,2212)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          2252..2377
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          2428..2708
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          2797..2969
                     /region_name="PKS_DH"
                     /note="Dehydratase domain in polyketide synthase (PKS)
                     enzymes; smart00826"
                     /db_xref="CDD:214837"
     Region          3094..3514
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(3296..3297,3299,3320..3323,3348..3351,3375..3377,
                     3398..3399,3421..3422,3436,3463..3464)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(3399,3423,3436,3440)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          3556..3641
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          3660..4765
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:225858"
     Region          3663..4088
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Site            order(3835,3970,4010)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          4050..4167
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          4213..4511
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          4585..4753
                     /region_name="PKS_DH"
                     /note="Dehydratase domain in polyketide synthase (PKS)
                     enzymes; smart00826"
                     /db_xref="CDD:214837"
     Region          4880..5311
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(5093..5094,5096,5117..5120,5145..5148,5172..5174,
                     5195..5196,5218..5219,5233,5260..5261)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(5196,5220,5233,5237)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          5353..5438
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     CDS             1..5532
                     /gene="aveA3"
                     /coded_by="complement(AB032367.1:33436..50034)"
                     /note="contains Ave module 7, module 8 and module 9;
                     multifunctional polyketide synthase"
                     /transl_table=11
ORIGIN      
        1 mdtsseklvd alraslkanq tlrarneqla aameassepi aivgmacrfp ggvcspeelw
       61 elvasggdai gefpagrgwd leglfdsdpd rsgtsyaryg gflyeagefd adffgispre
      121 alamdpqqrl lletsweafe ragidplsmr gsrtgvfagv myhdygsrlg tipegfegyi
      181 gngsggavas grvaytlgle gpavsvdtac ssslvalhla cqslrsgect lalaggvtvm
      241 stphlfvefs rqrglsvdgr cksfaggadg tgmgegvgml lverlsdavr lghrvlavlr
      301 gsavnqdgas ngltapngpa qervirqala naglsvadvd vveghgtgtt lgdpieaqal
      361 latygqragn rplwlgsvks nighaqaaag vggvikmvma lregvlprtl hvdepspqvd
      421 wsagavrllt eavpwpgdaa grlrragvss fgvsgtnahv ileeapaagg cvagggvleg
      481 apglaisvae svaapvavsa pvaesvpvpv pvpvpvpvsa rseaglraqa ealrqyvavr
      541 pdvsladvga glacgravle hravvlaadr eelvqglgal aagepdrrvt tghapggdrg
      601 gvvfvfpgqg gqwagmgvrl lasspvfarr mqaceealap wvdwsvvdil rrdagdavwe
      661 radvvqpvlf svmvslaalw rsygiepdav lghsqgeiaa ahvcgalslk daaktvalrs
      721 ralaavrgrg gmasvplpaq eveqligerw agrlwvaavn gprstavsgd aeavdevlay
      781 cagtgvrarr ipvdyashcp hvqplreell ellgdispqp sgvpffstve gtwldtttld
      841 aaywyrnlhq pvrfsdavqa laddghrvfv evsphptlvp aiedttedta edvtaigslr
      901 rgdndtrrfl talahthttg igtpttwhhh ythhhthphn hhldlptypf qrqhywldap
      961 tgagdvaaag lepaehplla atvqladtdg clltgrlslr shpwlgdyev ggavllsgsa
     1021 fvelavqvge rvgctrieql tvhaplvvpv gggvsvqvgv aaadgegrrl vsvyarggsa
     1081 cggggasggv wtchasgvlv eaaagggvvv dglagvwppr gavavdvdgv rdrlagagcv
     1141 lgpvfsglra vwrdggdlla evclpeeawg daagfglhpa lldgvvqpls vllpggtgfg
     1201 egagfgegvr vpavwggvsl hragvtgvrv rvwavgrggg reavsvvvgd eagvpvasvd
     1261 rlelrpvdmg qlravsvsag rrgslyavqw aevgpvpvcg qawawhedvg esgggpvpgv
     1321 vvlrcpdaga gggggggvge vvggvlgvvq gwlglerfag srlvvvtrga vvagqedgpv
     1381 dvvgaavwgl vrsaqaehpd rfvlldldtd tdtgtdldtg agagagagwg vdgghvaavv
     1441 acgepqlavr gervlaarlt rlessvdvpa qrsgdvagre vlpwlsggsv lvtggtgvlg
     1501 aavarhlagv cgvrdlllvs rrgpdapgae glraelaalg aevrivacdv gerrevvrll
     1561 egvpagcplt gvvhaagvld datiasltpe rlgtvfaakv daallldelt rgmelsafvl
     1621 fssaagilgs agqgnyaaan aaldalayrr raaglpgvsl awglweeasg mtghlagtdh
     1681 rriirsglhp mstpdalalf daalaldrpv llpadlrpap plppllqdll patrrrttrt
     1741 tttggadnga qlharlagqt heqqhttlla lvrshiatvl ghttpdtipp drafrdlgfd
     1801 sltavelrnr lsrttglrlp ttlafdhpnp ttlthhlhtq llgsdstasi papraaavpa
     1861 dqdepvaiig macrypggvt saeelwella sgrdtvgefp tdrgwdleal fdpepgrpgt
     1921 sytrcgsfly dagefdagff gisprealam dpqqrlllea sweameqagi dpttvrgsqt
     1981 gvfaglipqa ygprlhenaa adtegyvltg tsgsvasgri sytfgfegpa vsvdtacsss
     2041 lvalhlacqa lragecsmal aggvtvmssp gafvefsrqr glaadghcka fsaaadgtgw
     2101 gegvgmllve rlsdarrngh rvlavvrgsa vnqdgasngl tapngpsqqr virqalanag
     2161 lsagdvdave ahgtgttlgd pieaqallat ygqdragegp lwlgsvksnv ghtqaaagva
     2221 gvikmvmalr ngllprtlhv depsphvdws agavqlltet vpwpggegrl rragvssfgv
     2281 sgtnahvile eapahnipsd tpaddvpggp pagedagsge eaaagspgvw pwlvsaksqp
     2341 alraqaqalh ahltdhpgld ladvgytlah aravfdhrat liaadrdtfl qalqalaage
     2401 phpavihssa pggtgtgeaa gktaficsgq gtqrpgmahg lyhthpvfaa alndicthld
     2461 phldhpllpl ltqdpntqdt ttleeaaall qqtpyaqpal fafqvalhrl ltdgyhitph
     2521 yyaghslgei taahlagilt ltdattlitq ratlmqtmpp gtmttlhttp hhithhitah
     2581 endlaiaain tptslvisgt phtvqhittl cqqqgiktkt lptnhafhsp htnpilnqlh
     2641 qhtqtltyhp phtplitant ppdqlltphy wtqqarntvd iatttqtlhq hgvttyielg
     2701 pdntlttlth hnlpntpttt ltlthphhhp qthlltnlak ttttwhphhy thhhnqphth
     2761 thldlptypf qhhhywlest qpgagnvsaa gldptehpll gatlelaegd gclltgrlsl
     2821 rthpwlagha vggvvllpgt afaelalhag esvgcdhvde ltlhtplvip evgdvtlqva
     2881 iaapdesgrr mmtihsrgeg gsggadasas awtrhaagvl spakdddtas yellagpwpp
     2941 vgatpvdlnt aydqmadagf ayglafqglr aawrygddil vearlpeevs gdaaayglhp
     3001 alldaalqgt gllsvagpgt pvvphvwngl rfrthgavsv raclstlgat gaavcvritd
     3061 dtgvpvasvd rlelrpvdmg qlravsvsag rrgslyavqw aevgpvpvcg qawawhedvg
     3121 esgggpvpgv vvlrcpdaga dggggggvge vvggvlgvvq gwlglerfag srlvvvtrga
     3181 vvagpedgpv dvvgaavwgl vrsaqaehpd rfvlldldtd ldsgadadag neagmgsgld
     3241 ggrvaavvac gepqlavrge rvlaarltrl espvdvsgre vlpwlsggsv lvtggtgvlg
     3301 aavarhlagv cgvrdlllvs rrgpdapgae glraelaalg aevrivacdv gerrevvrll
     3361 egvpagcplt gvvhaagvld datiasltpe rlgtvfaakv daallldelt rgmelsafvl
     3421 fssaagilgs agqgnyaaan aaldalayrr raaglpgvsl awglweeasg mtghlagtdh
     3481 rriirsglhp mstpdalalf daalaldrpv llpadlrpap plppllqdll patrrrttrt
     3541 tttggadnga qlharlagqt heqqhttlla lvrshiatvl ghnapemipv dsafrdlgfd
     3601 sltavelrnr lgeatglrlp tslvfdqpna atlarhlrre lmgddaeget psqvalhqva
     3661 adepiaivgm acrfpggvcs peelwelvas ggdaigefpa grgwdleglf dsdpdrsgts
     3721 yaryggflye agefdadffg isprealamd pqqrlllets weaferagid plsmrgsrtg
     3781 vfagvmyhdy aarlhhvpeg fegliangsa gsvatgrvay sfglegpavt vdtacssslv
     3841 alhwaaqalr agecsmalag gvtvmsspgt fvefsrqrgl aadgrckays aaadgtgwae
     3901 gvgmllverl sdarrnghrv lavvrgsavn qdgasnglta pngpsqqrvi rqalanaglt
     3961 padvdavegh gtgttlgdpi eaqallaayg qhrphhrplw lgslksnigh aqaaagvggv
     4021 ikmvmalrng llpqtlhvde ptpqvdwstg avqlltqpvp wpadpagrpr hagvssfgvs
     4081 gtnahvilee apaaaggaag ggvsvgapnp alpvaesepv pvpvpvsars eaglraqaqa
     4141 lrqyvaarpd mspadigagl argravlehr avilaadree laqaltalaa gephphittg
     4201 htrgsdrggv vfvfpgqggq wagmgltllt sspvfaehid acekaltpwv pwsltdilhr
     4261 dpddpawqqa dvvqpvlfsi mvslaalwrs ygiepdavlg hsqgeiaaah icgalslkda
     4321 aktvalrsqa laavrgrgam vslplpaqdv qqliserweg qlwvaalngp hsttvsgdtt
     4381 aveellthca dtglrakrip vdyashcphv qplhdellhl lgditpqpst mpffstvvgh
     4441 lvwytttlda aywyrnlhqp vrfshaiqtl tddghrpfie isphptlvpa iedttentte
     4501 nitatgslrr gdndthrflt alahthttgi rtpttwhhhy tqthphphnh hldlptypfq
     4561 hqhywlqppt tttdltttgl tpthhpllta tltlannntq lltgrlslrt hpwltdhtvv
     4621 gttlvpgtal lelalqattt dhleelalht plvipregav dvqvhinppd dtdtrsltiy
     4681 srsenapaaa pwrhhatavl gtktsrietg rshddlsmwp pagavrcade elaalygdye
     4741 angfvygpaf rgltaawrlg devfaevrlp eqvhgeasay nlhpalldaa lhaaafapsg
     4801 slpqgsvpfs ftgvtlhaan asslrvrlsp adpnsghaav svlvtddtgt pvasvealav
     4861 rplaadelra aeravqrael fdmkwvevps dvlvsggasv vvldgaddlv glaaeedgvp
     4921 gvvvlrcpda gadggggggg vgevvggvlg vvqgwlgler fagsrlvvvt rgavvagped
     4981 gpvdgpvdvv gaavwglvrs aqaehpdrfv lldldtdlds gadrdagnea gmgsgldggr
     5041 vaavvacgep qlavrgervl aarltrlesp vdvsgrevlp wlsggsvlvt ggtgvlgaav
     5101 arhlagvcgv rdlllvsrrg pdapgaeglr aelaalgaev rivacdvger revvrllegv
     5161 pagcpltgvv haagvlddat iasltperlg tvfaakvdaa llldeltrgm elsafvlfss
     5221 aagilgsagq gnyaaanaal dalayrrraa glpgvslawg lweeasgmtg hlagtdhrri
     5281 irsglhpmst pdalalfdaa laldrpvllp adlrpapplp pllqdllpat rrrttrtttt
     5341 ggadngaqlh grlagqtheq qhttllalvr shiatvlght tpdtippdra frdlgfdslt
     5401 avelrnrlsh ttglrlpttl afdhpnpttl thhlhtqlvs kgltaaaepd aattppglps
     5461 llselerlea vvlssttssa aplddgartr lasrlhslaq klngddtapd laetsdeemf
     5521 alidrevgfe sq
//

LOCUS       BAA84479                4881 aa            linear   BCT 18-SEP-1999
DEFINITION  type I polyketide synthase AVES 4 [Streptomyces avermitilis].
ACCESSION   BAA84479
VERSION     BAA84479.1
DBSOURCE    accession AB032367.1
KEYWORDS    .
SOURCE      Streptomyces avermitilis
  ORGANISM  Streptomyces avermitilis
            Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
            Streptomyces.
REFERENCE   1  (residues 1 to 4881)
  AUTHORS   Ikeda,H., Nonomiya,T., Usami,M., Ohta,T. and Omura,S.
  TITLE     Organization of the biosynthetic gene cluster for the polyketide
            anthelmintic macrolide avermectin in Streptomyces avermitilis
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 96 (17), 9509-9514 (1999)
   PUBMED   10449723
REFERENCE   2  (residues 1 to 4881)
  AUTHORS   Ikeda,H., Nonomiya,T., Usami,M., Ohta,T. and Omura,S.
  TITLE     Direct Submission
  JOURNAL   Submitted (13-SEP-1999) Haruo Ikeda, School of Pharmaceutical
            Sciences, Kitasato University, Microbial chemistry; 5-9-1
            Shirokane, Minato-ku, Tokyo 108-8641, Japan
            (E-mail:ikeda@mc.pharm.kitasato-u.ac.jp, Tel:+81-3-5791-6242,
            Fax:+81-3-3444-6197)
FEATURES             Location/Qualifiers
     source          1..4881
                     /organism="Streptomyces avermitilis"
                     /db_xref="taxon:33903"
     Protein         1..4881
                     /product="type I polyketide synthase AVES 4"
     Region          3..26
                     /region_name="Docking"
                     /note="Erythronolide synthase docking; pfam08990"
                     /db_xref="CDD:286127"
     Region          34..457
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Region          36..459
                     /region_name="PKS_KS"
                     /note="Beta-ketoacyl synthase; smart00825"
                     /db_xref="CDD:214836"
     Site            order(206,341,380)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          420..>505
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          578..879
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          987..1461
                     /region_name="KR_1_SDR_x"
                     /note="ketoreductase (KR), subgroup 1, complex (x) SDRs;
                     cd08952"
                     /db_xref="CDD:187655"
     Site            order(1220..1221,1223,1243..1246,1271..1274,1299..1301,
                     1322..1323,1345..1346,1360,1387..1388)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187655"
     Site            order(1323,1347,1360,1364)
                     /site_type="active"
                     /db_xref="CDD:187655"
     Region          1483..1568
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1590..2681
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:225858"
     Region          1591..2015
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Site            order(1763,1898,1938)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          1978..>2063
                     /region_name="KAsynt_C_assoc"
                     /note="Ketoacyl-synthetase C-terminal extension;
                     pfam16197"
                     /db_xref="CDD:292814"
     Region          2139..2436
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          2525..2610
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          2635..3843
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:225858"
     Region          2636..3059
                     /region_name="PKS"
                     /note="polyketide synthases (PKSs) polymerize simple fatty
                     acids into a large variety of different products, called
                     polyketides, by successive decarboxylating Claisen
                     condensations. PKSs can be divided into 2 groups, modular
                     type I PKSs consisting of one or...; cd00833"
                     /db_xref="CDD:238429"
     Site            order(2808,2943,2983)
                     /site_type="active"
                     /db_xref="CDD:238429"
     Region          3263..3557
                     /region_name="PKS_AT"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes; smart00827"
                     /db_xref="CDD:214838"
     Region          3650..3827
                     /region_name="PKS_DH"
                     /note="Dehydratase domain in polyketide synthase (PKS)
                     enzymes; smart00826"
                     /db_xref="CDD:214837"
     Region          3955..4441
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(4191..4192,4194,4215..4218,4243..4246,4270..4272,
                     4293..4294,4316..4317,4331,4358..4359)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(4294,4318,4331,4335)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          4460..4557
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          4672..4873
                     /region_name="PKS_TE"
                     /note="Thioesterase; smart00824"
                     /db_xref="CDD:214835"
     CDS             1..4881
                     /gene="aveA4"
                     /coded_by="complement(AB032367.1:50212..64857)"
                     /note="contains Ave module 10, module 11 and module 12;
                     multifunctional polyketide synthase"
                     /transl_table=11
ORIGIN      
        1 maneeklrdy lkrvtadlln vrrrlqqies geqepiaivg macrfpggve saedfwelia
       61 sgrdavgefp vdrgwdveaf ydpepgrags sytrrggfle gaaefdagff gisprealam
      121 dpqqrlmlev swealeragi dpatlrgsrt gvfaglmsqd yatrllsvpd dlagylgngn
      181 agsilsgrva ytfgfegpav tvdtacsssl valhlacqsl rtgessfala ggvtvmstpg
      241 mfvefsrqrg lspdgrckay asaadgtgms egvgilller lseaerrghr vlavvrgsav
      301 nqdgasnglt apngpsqqrv irqalacagl svadvdvveg hgtgttlgdp ieaqallaty
      361 gqragdtpvw lgsvksnigh aqaaagvagv ikmvmalrag vlprtlhvde pssqvdwssg
      421 svrvladeve wpgvegrlrr agvsafgvsg tnahvileea sggagggagr lqelgpgvvs
      481 gsgvvpwvvs arselalrgq arrlrgvvav gggadgvgvs pagvgralvs ersvfehrav
      541 vvaedrdefl haldalaggr pvpgvvegrt tsgelavlfa gqgtqragmg relyeaypvf
      601 aqaideicae adtartdpga pglrdvlfap qdspegrlie dtgfaqpalf afevalfrll
      661 etwgltpdyv lghsvgelaa ahvagmlcla davalvvarg rlmqglpsgg amvaieased
      721 eilplpdeya srvahaavng prsivlsgde davldlaqqw aargrrtrrl rtshafhsph
      781 mdamlgdfrr aaeqvtfsap ripvvsnvtg aplpaetmct pdywvehars tvrfadgisw
      841 lqeqgvttcl eigpdgtlsa laqdslsapa raipalrpdq pearsvmtal aelfvagtav
      901 ewagvfegta revgdgcgve lptyaferer fwldveegsa ggsgvsgmwg gplweavecg
      961 dagvvasllg vdegaslgav vsalgewgrv rherevvdgw ryrevwrpvs gggvgglsga
     1021 wlvvsegeag pvdvvaegle rcgarvvrve veagcvsrev laghlreavd geavggvvsl
     1081 vgwgsgvvqa gvasvglvqa lgdvgvgarl wcvtggavsv ggrdavwgpa sgvvwglgrv
     1141 vgaeapdrwg glvdvpelvd ervvdglvgv lagvgggges efavrssgaf vrrlvraple
     1201 eavaerewrp rgtvlvtggt gelgahvarw marrgaehll lvsrrgesaq gveelradlm
     1261 glgarvsvva cdaadreala evlrsavpae cplgvvvhaa gvvddgvleg lsservtgvl
     1321 rakalaawnl heltrgadls gfvvfssaaa tfgpagqgsy aaanayveai vrhrrgeglp
     1381 glavawgpwa gggmaegavg qmrrrglaam tpetalvalg qaldhdetcv tvadidwdrf
     1441 tanslpgsrl splisdipea rlarettgld tataspdsfs arlkamdtae qeralldlvr
     1501 tyaatvlghs tptavrpera frdlgfvsvs avelrnrlna vtglllpttl ifdyptpsal
     1561 agylkeqlee gaggqrdiap pvpasrvdvd epiaivgmac rfpggvesae dlwelvasgr
     1621 davgefpvdr gwdveafydp epgragssyt rrggflegaa efdagffgis prealamdpq
     1681 qrlmlevswe aleragidpa tlrgsttgvf agmcsqdyad lvrratedle gyamtglsss
     1741 vtsgrvaytl glegpavtvd tacssslval hlacqalrsg ecslalaggv tvmstpgafv
     1801 efsrqrglsp dgrckaygsg adgvgwaegv gvllverlse aerrghrvla vvrgsavnqd
     1861 gasngltapn gpsqqrvirq alacaglsva dvdvveghgt gttlgdpiea qallatygqg
     1921 rsgerpvwlg svksnighaq aaagvagvik mvmalragvl prtlhvdeps sqvdwssgsv
     1981 rvladevewp gvegrlrrag vsafgvsgtn ahvileeasg gadggagrlq elgpgvvsgs
     2041 gvvpwvvsar selalrgqar rlrgvvavgg gadgvgvspa gvgralvser svfehravvv
     2101 aedrdeflha ldalaegapt agvvqgvagp aadgkiamlf ggqgthwegm aqellgsspv
     2161 faqqmsdcaq alepyldwsl ldvlrgapda pplqrvdvvq pvlfavmvsl aalwrsygvh
     2221 pdavaghsqg eiaaayvaga lslddaarvt alrsqalaal agqgamasvg lpvekleprl
     2281 atwgdrlvia avngarsavv sgepeavdal veelshedvp arrlmvdwas hspqveaiqg
     2341 rllellapir artgdvpfys tvtgeridgt eldadywyrn lrqvvrfrda tqalvraght
     2401 vfieacphpa vavgvqetld emgdldslvv gslrrgeggl rrflmsvael fvggvavews
     2461 gvfgsvgrgv aggcgvelpt yafererfwl dvegaprgsg vsgqwggqls eavdtvrggm
     2521 lrdclagldp aaqaetvldl vlthaaavlg hgtadavvpe rafrdlgfds ltavelrnrl
     2581 ntatglrfpr tlvfdhprpv alaahiheql sggspttgta lalalrapap rvdvdepiai
     2641 vgmacrfpgg vesaedfwel iasgrdavge fpvdrgwdve afydpepgra gtsytrcggf
     2701 lqgaaefdag ffgispreal amdpqqrlml evswealera gidpatlhgs ttgvfagvsq
     2761 qdyaellrrg tqdhegyalt gvsnsvvsgr lsytfgfegp avtvdtacss slvalhlacq
     2821 alrsgecsla laggvtvmst pgafvefsrq rglspdgrck aygsgadgvg waegvgvllv
     2881 erlseaerrg hrvlavvrgs avnqdgasng ltapngpsqq rvirqalaca glsvadvdvv
     2941 eghgtgttlg dpieaqalla tygqgrsger pvwlgsvksn ighaqaaagv agvikmvmal
     3001 nhellptslh idepsphidw ssggvrllte pvpwqqngrp rragvsafgv sgtnahviie
     3061 qapveahvis epvpaeahvi veqapveaph vvdatgpadl tepqeeaaep ecvadavtem
     3121 saepecvada msemsaecva eavsdksaep ecvadamsdk pallpipwll sakseralrg
     3181 qarrlrqfaa rasdarpadv ahalaaqrsv fdhravvvae drdgflqald alaegrsadg
     3241 liegsvgprg ghsgrrrgkt amlfagqgtq rvgmgrqlya ahpayadald qvlaeldghl
     3301 dqplrpliha sadladvada advldrtrya qpalfavqva lfrhlerlgv radfvaghsi
     3361 gelaaahvag vlplaaacrl vaargrlmeq lapggamvav raseaearqa ldgrearvsv
     3421 aavngpasvv fsgaedevgn madwfaergr rvkrlrtgha fhsplmdpml eefqqvaasl
     3481 tysepaipmv stltgdivaa gelsdpeywv rqvrrtvrfg daisrlhtdg vrtfmelgpd
     3541 gtlsalaeec leatadshpa dddtgtpqen llipllrpds pepgtlltgl arlhthgaaa
     3601 vnwpaalper drarhldlpt yafdhhrywv dtsaghpgdl saaglgtagh pllgsavala
     3661 esqellftgr lslrthpwla dhaifgtvll pgtailelav ragdevdcgt veeltlrtpl
     3721 vlpeqgsvil qlsvgapqgp qtpeeperrt falyareddg lssssaaatg tewtchatgv
     3781 ltgtarpaee htqepwppad aapvdldgwy eqlagaglgy gpvfqglrev wrrgdevfav
     3841 vtlpestegq aadaaryalh palldaalhp vvlrhegdaa adghgwlpfs wtgvtvaasg
     3901 astlhvrltv rtdedavgll atdasgrivi sagslafrpv saeqlqaart gyhdhlfrie
     3961 wrplhlpttp artadwalig pgarrtaavl erngaswqay pdpaalaeal aagapapgmv
     4021 viscepdgas aptdsaltds altdsapags apadstalad atrqattrvl allqewvade
     4081 rlaacrlall thgsvtatpd epvsdlahaa vwglvrsvqt enpdrfllad tddtdasrna
     4141 lpllagepqi alrngavrip rmtrvpvrqp qpsttdadwd peatvlitgg tgvlgrlvar
     4201 hlatahgvrh lllatrrgta adgaadlvae laglgaeatv aacdigdraa vaalldqvpa
     4261 qhplkaviht agvvddgilt sltpermeav lhakafgaah lhdltrdagl ttftvfssaa
     4321 asfgspgqgn ytaanaflda lmqhrhtqal pgrslawglw geadgmtrnl agtdfarmar
     4381 ggllplsnaq glalldtadr lgpfgdglll atrldaatlh aqatagalpr ilhgliripa
     4441 rrsadhgiat dtpatlrerl agltipaqrt glllelvrth aaavlghpts avtaadgalp
     4501 ddlvpadtef rdlgfdslta velrnrinav tglrlpatli fdqpspaala dhlatrltae
     4561 agtpdepapa aaaagagsag saetgqqrst gsekqqtrgg tstetveslf wighdtrrie
     4621 esmallsaas ffrpaftdps dipeptfvrl aqgearaqge alargetrpa liclptvaav
     4681 ssvyqysrfa aglnghrdvw yvpapgfleg eplpsgigav trmfadaivr ftdgapfala
     4741 ghsaggwfvy avtshlerlg vrpeavvtmd aylpddgiap vasaltseif drvtqfvdvd
     4801 ytrlvamggy frifsgwspp dittpalflr grdgeqmppp wgvphtvldi qgnhftmleq
     4861 fadstarhvd ewlteiasvr r
//