ID D9WAY9_9ACTN Unreviewed; 2115 AA.
AC D9WAY9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:EFL20783.1};
GN ORFNames=SSOG_00495 {ECO:0000313|EMBL:EFL20783.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL20783.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL20783.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL20783.1,
RC ECO:0000313|Proteomes:UP000003963};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG657754; EFL20783.1; -; Genomic_DNA.
DR STRING; 457427.SSOG_00495; -.
DR HOGENOM; CLU_000022_35_2_11; -.
DR Proteomes; UP000003963; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd08952; KR_1_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 6.10.140.1830; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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; IPR041618; PKS_DE.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
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; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF18369; PKS_DE; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 3.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 147..222
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 244..670
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1690..1765
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1784..2115
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 2087..2115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2089..2107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2115 AA; 219748 MW; 17AC565A9FDBB399 CRC64;
MTGVLGNAGQ AAYGAANAYV DALAHHRRGL GMPATSVAWG PWSGDGMAAD GRVVEHFRRL
GVRPLDPDRA IAALRSALDD GRAARVVVDV DWERFAASVA FTRPGPLIAE LPEVADQART
RVADPSAPAG GELALRLRGR PAAEQDRMLL DMVLSQVAAV LGHATPATID PARAFKELGF
DSLTAVSFRN RLATATALRL PTTLIFDHPT PAALTAFLRG QVLGVTADEA GHTDAALAPL
GAGDDPIVIV GMGCRFPGGA ASPEELWDLL STARDGLSPF PVDRGWDVDG LFHPDPAHSG
TSYVRVGGFL HDAAEFDAEL FGISPREALA MDPQQRLLLE TAWEALERAG VDPLSLRGSA
TGVFAGTNGQ DYQHTARGPA ADVEGYVTTG SAASVLSGRV SYALGLEGPA VTVDTACSSA
LVALHLAAQA LRAGECRMAL AAGATVMATP DLFVDFSRQR ALAADGRCKA FAEGADGTGW
SEGAGVLVLE RLSDAQRLGH PVLAVVRGSA VNQDGASNGL TAPNGPSQQR VIRQALAAAR
LSPADVDAVE AHGTGTSLGD PIEAQALLAT YGQGRDGGEP LWLGSVKSNL GHTQAAAGAA
GLIKMVLALR EQRLPKTLYA DEPSSRVDWE SGTVRLLTEA REWPSGDRPR RAGISSFGIS
GTNAHIILEE APQAAPAAVE EPSAELPIVP WVLSGRTAQA VRAQAGRLAA LLDAGDGSPL
DIGFSLGTTR ATLEHRAVVL GGDLDALRSG VTALADGDDA VISGVVGEGR TGWMFTGQGS
QRAGMGRELY AQFPVFARAL DEVCAQLDAA LRGEPGFEVP VRDVLFAPEG SYEAGLLDGT
GYAQTGLFAV QTALVELLRS WGMSPDVVFG HSVGEFVAAY TAGVFELADA ARLVAGRARL
MQALPTGGAM AAIEATEAEA VEVLGTLLDG ERLAIAAVNG PDAVVISGDE AVVEQAMASA
QEQDRRVSRL RVSHAFHSPL MEPMLAEFAE IAATIDYRQP TLPAISTVTG DLVGGEDWVT
PEYWVHQVRR PVRFHDAVVT ATAEHAATRL LELGPAPVLS ALAQSAAGST VAVSALREGR
AEAETVFAAV AEMFVRGADV DWPGVFAGTG ARRVDLPTYA FQRRRFWLRD QATEQPERAV
GGGAEGIETE FWNLVERGDA DALAGRLGVE SAAPLDAVLP MLSDWRQRQR ERSELADWRY
RITWKPVTLP NTGRLSGTWL VAVPEADEAR AEPCVRALRA GGAEVRVLPV AATDTADTLA
DRLRTTADGA AAGIVSLLAE GSDEPSTVTA TTLTLIHALG DTELPVWCVT RSAVSVGSGE
HLANPAQAQL WGFGRTVALE QPRRWGGLVD VPENADEKAW TRLVSVLAAA HGDGDGEDQL
AVRPSGVFAA RVVRDRAGAP DGEGWRPRGT VLITGGTGAL GGHVGRWLAS RGAEHLVLVS
RRGARAPGAK ELCEELTALG ARVTVTDCDI TDREALAAVL DGVPEDAPLT GVVHTAGVLD
DGLATDLTQE RLAGVLAAKA GAARHLHELT AELELDAFVL FSSIAGALGN AGQSAYAAGN
TYLDALAQHR RGLGLPATSV AWGPWGESGM VTDGGVEEYL RRRGLKALPP RRAMAALQQA
MAEGRVCAML ADVDWQRFAP SFTSSRPSAL IGDLPEAAAA RAADSPAHAA PTDGELARRL
SGLSAQEQGR LLLDLVRSQV AAVLGHASPT AIAPERPFKD LGFDSLTAVD LRNRLGGATA
LSLPTTLIFD YPTPAALTAF LRGQLLGGSV DRDGTPEATA SVADEPIAIV GMGCRFPGGV
ASPEALWDLV TSGGERMSPF PDDRGWDVPG LLDATSAAMG TEYAGVGGFV PDVADFDAEL
FGISPREALA MDPQQRLLLE TAWEALERAG IGPLSLRGSS TGVFAGISAN GYGGFAHEDG
GESAGYLQTG STPSVASGRL SYVLGLEGPA VSVDTACSSS LVSLHLACQA LRAGECDTAL
AGGVTVMATP ATFVEFSRQR GLAPDGRCKA FAEAADGTGW SEGAGVLVLE RLSEARRRGH
EVLAVVRGSA VNQDGASNGL TAPNGPSQQR VIRLCAVLGA ALGVRRGRGG GARHGDAAGR
PDRGAGAARD VRSGP
//
