ID D7BSN8_STRBB Unreviewed; 3991 AA.
AC D7BSN8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE SubName: Full=Putative type I polyketide synthase {ECO:0000313|EMBL:ADI11535.1};
GN Name=nanA3 {ECO:0000313|EMBL:ADI11535.1};
GN OrderedLocusNames=SBI_08417 {ECO:0000313|EMBL:ADI11535.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI11535.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI11535.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI11535.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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DR EMBL; CP002047; ADI11535.1; -; Genomic_DNA.
DR RefSeq; WP_014180985.1; NC_016582.1.
DR STRING; 749414.SBI_08417; -.
DR KEGG; sbh:SBI_08417; -.
DR PATRIC; fig|749414.3.peg.8662; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_8_11; -.
DR Proteomes; UP000000377; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 2.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 3.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR036299; Polyketide_synth_docking_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; INACTIVE PHENOLPHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PKS1-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 2.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF21089; PKS_DH_N; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 2.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 2.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 5.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..460
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1782..1857
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1884..2253
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3830..3905
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 462..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3991 AA; 414360 MW; CB01EC27ED2CEE3A CRC64;
MTTETNEERL VDYLKRVAAD LHDTRARLRE VEDGQREPVA IVAMACRYPG DVASPEALWD
LVAARRHAMT AFPDNRGWDL ERLFHPDPDH PGTSYAREGG FLHDADLFDP EFFGISPREA
AVVDPQQRLL LEVAWEALER AGIAPGSLKG APVGVYAGTA LPGFGTPHID RAAEGYLVTG
NAPSVLSGRV AYTLGLEGPA VTVDTACSSS LVAMHLAAQA LRQGECELAL AGGVTVMTTP
YVFTEFARQR GLAADSRCKA FSEGADGTAF AEGAGLLVLE RLSDAQRNGH QVLAVMRGSA
INQDGASNGL TAPNGLAQQR VIRQALAGAR LSPADVDAVE AHGTGTTLGD PIEAQALLAT
YGQERPEGRP LWLGAIKPNL GHTQGAAGVA GVIKMVMALR NASLPALLHA DRPTSVVDWD
GGAVRLRAEP VAWPAGDRRR RAGVSSFGIS GTNAHLILEE APPQPVPEDT ADTADTADTP
QRPEGTVVPW VVSARGAASL RTQAAALAEH MAAHPGTLVD AIGWSLATTR SPLDHRAVVL
GADREELSAR LADLAEGRTH PDVTRASAPA RLGGSAFLFT GQGSQRPGMG AQLYRAYPAF
AAAFDEACAA LDPHLGRSLR ELVFAPADAD GDGDADRASA LDATEVTQAA LFAVEVALYR
LVESFGVVPG YLAGHSVGEL VAAHIAGVLS LPDAARLVAA RGRLMQALPE GGAMVALEAA
EEEVAPLLAG RADQVALAAV NAPTSVVVSG DEEAVEEIAR TIRERGHRTR RLRVGHAFHS
PRIDPMLEEF RQVAASLTYS QPRIAVVSNV TGALAGAEQL CDPDYWVRHA RQPVRFRDGI
AALRAEGVTR FLELGPDAVL TAMARDCLTS EAAPEVAAGE SAQDAGTSSG PGAPVLATVL
RKGRDEPRTL LTALAQLHVD GESVDFSAAF PPATQATDLP TYRFDRRRYW RGAPPRPPAP
QAEADVRAAG LEASDHPLLR AALEPADGGL LLTGRLSLRG QPWLADHAIV DAVPLPGTLF
VELALQAGER VGCDLIDDLT LEAPLLLPPV GAVDLQVAVG APGAAGRRAV TVYSRPSGGG
SEGSEDPGVA DEPGDGPSGA YGPWRRHATA TLSATATGAA TGVPEPAAPP AQWPPAGAEA
IDVAGLYERL AAEGYRYGPA FTGLRTAWRV GEEMFAEVGL APGQRGDGGA YAIHPALLDA
ALHPIGALFT GVDQAGGAPG TVRLPFSFGG VRLLARGASR LRVRITPTGP DTVTMRLSDD
TGAEVVAVDS LTLRAVSAQR WRSGAVPADR PLYRLGWDAF ALPAAATTAP DRWAVPAADD
TNATDAATAS LPAEHVARHP DLAALSASVA AGAPAPDLVV MACLGAPYDT SDDGDEPPSR
VRTATHRVLA RLREWLTDDA LATSRLVVLT AGAVAADPAD APPDLAGAAV LGLLRAAQAE
HPGRIVLVDT DGTSASRDAL AAAVAAAVAA GEWQLALRDG RALVPRLVLA HPDPDAAPVL
LDPDGTVLVT GGTGSLGRLL ARHLVENHGA RHLLLVSRSG AAAEGIEAFA AGLAADVRIE
SCDTADPEAL AALLATVPGE HPLTAVVHTA GVLDDGVVTS LTPEQLDAVL APKVDAAWQL
HRLTRGADLA SFVLFSSAAS VLGSGGQGNY GAANAFLNAL AEHIRAAGGP ATSLAWGLWG
VDEGMTEHLA TADRARMARS GTAAMSGEAG LARFDAALAT ALPVLVPARF DLAVLREQAA
TGALPPLLRR LVRLPVRTAA AVAASPSWAG RLAGLPETEQ DRVIGELIRD RIAAVLAHPE
PETLELGRTF AQLGLDSLTA LELRNAIHEA TGVRLPATAI FDYPTPETLV SHLRTELLGA
TAATAATTPL SPGAGAPARS GSADDPVVIV GMACHYPGDV HSPDELWRLV ADGVDAIGPF
PEDRGWDVAG LYDPDPERTG KSYTREGGFL PEAALFDAEF FGISPREALA TDPQQRLLLE
TAWQAFEHAR IDPAALRGSR TAVVTGIMYD DYGARFLGRI PEGYEGQIMT GSTPSVASGR
VAYTFGLEGP TLTVDTACSS SLVAMHLAAQ ALRQGECDLA LAGGVTVMAT PNTFIEFSRQ
RGLAPDGRRR PSNVIGQALA VAGVDPAGVD VVEAHGTGTT LGDPIEAQAL LATYGRNRPA
GQPLWLGSIK SNIGHTQAAA GAAGIIKMVM ALRHGRLPAT LHVDEPSPHV DWASGSVRLL
TEATDWPEAD RPRRAAVSSF GISGTNAHII LEQAPDQPEP LPEQSASAAA GGIVPFVLSA
RTAEALRAQA ANLAARLPSA EVAEVGWSLA TTRSAFEHRA VIVAEDRDAL LAGLEKLAAD
EPDPAVVAGA ATTAAAGPVF VFPGQGSQWR GMGVELLDTS PVFAARIAEC ERALAPYVDW
SLTAVLRGAD TTTDPHRVDV VQPTLWAVMV SLAALWQHLG IAPAAVIGHS QGEIAAACVA
GALTLDDAAK VVALRSQALR ALAGHGTMAS LTLGADDTAG LLEELGEQAD DVTLAAANGP
ATTVISGAVE QIATVLAAAE ARGARTRTID VDYASHGPHV DRIREDIVSA LSGLAPTVSE
VAFYSTVTAE RLDTVGLDAD YWFTNLRRPV RFADTLATLL AHGHRHFIEV SPHPVLIPGM
QDGFEAADAA ATAVPTLRRD QGGPHQLAQA VARAYTAGLA IDWAPWYPAE PHTTDLPTYP
FQRRRYWLGM DGGPGDLRSA GLISVAHAQL GAAVELADGG LVMTGRLPAA GSGGWLDDHV
VADTPLVPGT ALVEWVLRAA DEAGCGGIEE LALHVPMTLP ASGGLRIQVV AYAPDGDGRR
EVRVHSRPDA EDGWSPWTCH ATGHLSPTAP TAPGAADPAQ AGVWPPRDAE QIDVADFYGR
AEAIGYGYGP AFRGLTAAWR QGDDLLAEVV LPEAAHEGSD GFALHPALLD AALHPLALDG
QGEDGQMRLP FAWSGVSLWA TGARAVRVRM SPLEHGFRLV VADAAGRPVL SAESVVVRPT
SAGQLRDAGA RRVDGLYEVA WVPLPPSSDT EAETETRGVE GWALLDGGPL PFDPSKAGSL
PRYADIDALL TAAALPSTVL VGVSGAVGAA GAEGDEDSAE VALAVTTGVL APARRWLETP
ELADARLVLV TRGAVAAAET DDGPDPAAAA VWGLLRSAQA ENPGRFLLCD IDDGAGPDDV
LGAVTRAVAL DEPQVAVRDG RVLTPRLECA GAAGLAPPPG APAWRLAADD TGTIDSVSVV
ACPEVLEPLA PGQVRIAVRA AGINFRDVLI VLGMYPDEGV FRGSEGAGVV LDVADDVTSV
AVGDRVFGLF EGAFGPVAVA DARAVVPIPP GWTDQQAAAV PTTFLTAWYG LVDLAGLKAG
ESVLIHAATG GVGTAAVQIA RHLGAEVYAT ASPGKHAVLE AMGIDEAHRA SSRDLDFEDA
FRTAAGGRGF DVVLNSLAGE YTDASLRLLT GGGRFIEMGK TDKRDAEQIA DTYPGVRYRF
YDLVPDAGLN RVAEMLTTLA GHFAQGVLAP PPVRAWPLTE ARQALRQMSQ ARHTGKYVLD
MPRTLGPDGT VLITGGTGTL GALVAEHLVT THHITHLHLL SRRGPDAPGA AELTARLTEL
GATVRITATD TADPQALRQA LDTVDRDHPL TGVIHAAGAL DDAVLTAQTP ERLASVWAAK
ATAAANLHRA TKDLPLAMFV IFSSAAGTLG TPGQANYAAA NAYCDALAVR RRQAGLPATS
IAWGLWAATS AMTGHLADAD LARMSRTGFT PLATPMALAL FDAAGRHGGA TPLALDLDPR
TLGAQPSDAV PAVLRTVAAA GAPVRRTAAV AQSTDWAGRL AALSAAERHR ELVNLVRTHA
ATVLGHSDPA ALRADTSFKE LGFDSLTAVE LRNRLSAATG LRLPAALVFD YPDAETMARF
LDQKLAPADR TEAAAVDHLA PVLNDLARLE STLGSHDVDG KARETIAGRL HALLSRLEGS
TASAADIDGE ALESASDDEM FALIDQQLGS S
//