ID D7CDZ7_STRBB Unreviewed; 2559 AA.
AC D7CDZ7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Putative type I polyketide synthase {ECO:0000313|EMBL:ADI04662.1};
GN OrderedLocusNames=SBI_01541 {ECO:0000313|EMBL:ADI04662.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI04662.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI04662.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI04662.1,
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).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP002047; ADI04662.1; -; Genomic_DNA.
DR STRING; 749414.SBI_01541; -.
DR KEGG; sbh:SBI_01541; -.
DR PATRIC; fig|749414.3.peg.1586; -.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_31_0_11; -.
DR Proteomes; UP000000377; Chromosome.
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; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.11460; -; 1.
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 Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
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; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF18369; PKS_DE; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 625..700
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 723..1149
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2405..2480
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 593..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2559 AA; 267739 MW; CA8832BA0D305901 CRC64;
MRFAASPDGV SWQDVGPALE ATRLSDDYGE RLRFTGAFGC GRGLGRGLRG HRRVAGGSAD
VCLPREADEI EARFWEAIEN EDLESLTTTL DISGDEPFNA VLPALSSWHR LRQEQSKLAG
WRYRISWQPL DKTPGSALSG TWLAVVPASH ADDEWAAEAV QALSAQGART IRLVVEADAG
RKRLAQQVSQ AVEGTSVAGV LSLLALDTAA HPGHPGVPSG LAGTLSLLQA LVDAGADTRL
WCVTRGAVSV GRADRQTGAV QTPVWGLGRV AALEHPDRWG GLLDLPQTLD TRAQERLCAV
LAGATVGGSP EDQLAIRPAG VFVRRLVRAP QNTAAGHSGW KPRGTVLVTG GTGALGGHVA
RWLAGHGAEH LVLTSRRGAD APGAAELTAE LTELRVGVTV AACDVADRAA LAELLASIPA
ERPLTAVVHV AGVLDDGVIE SLTVAHLERV LRSKVSAARH LDELTQHLEL DAFVLFSSVA
GALGNGGQAA YAAANTYLDA LALDRRQRGL PAVALAWGTW SGGGMVGGAI DERMSRRGLR
AMAPEVAIEA LGQVADRDEP FLAVADIDWP RFVTEFAATR RSRLFDELPE ARAGRAAERD
DATESHSGPG LAGRLADLAP VEQERLLLEL VRTHAAAVLG HAEADSVAAG RAFKELGFDS
MRVMELRNRL NVATGLRLAT GAVFDHPTAT LMAKHLRTEL VGDDAATATA APAPIPVALP
AADEPIAIVA MGCRFPGDVR TPEELWQLLA EGRDVISELP TDRGWDVEGL YDPDPDRSGK
SYTREGGFLH DAAEFDPAFF GISPREALAM DPQQRLLLET AWEALERAGI DPQSLKGTTT
GVFAGMTYQD YAARLHEAPN SVEGYLLTGK SSSVISGRIA YVLGLQGPAI TVDTACSSSL
VTLHLAAQAL RQGECSLALA GGVTVMAAPG MFIEFSRQRG LSADGRCKAF SAAADGTGWG
EGAGMLLLER LSDARRNGHP VLAVVRGSAV NQDGASNGLT APNGLSQQRV IRQALANARL
SAAEVDAVEA HGTGTTLGDP IEAEALLATY GQGRPEDRPL WLGSLKSNMG HPQAAAGAAG
VMKMVLAMQH GVLPRTLHVE EPSPEVDWEA GAVELLTEQR AWPETGRPRR AGVSAFGVSG
TNAHVILEQA PETVGEPVEP AEVPVVPVVP GVVPWVVSGR GVGALRGQTG RLLSHVDGFG
ELSPVDVGWS LASGRTAFEH RAVVVGDRDG LRAGLHALAR GESASGVVVG QGVGSGWMAV
LFSGQGSQRV GMGCELYGQY PVFAGAFDEV CGLLDKELAG HVERSVRDVI FGDDAVLLGQ
TVFTQAGLFA VEVALFRLVE SWGVVPEFVG GHSVGEIVAA HVAGVFSLED AVRLVAARGR
LMQALPAGGA MVAVQAAEDE VAPLLAEYEG RVGVAAVNSR TSVVVSGDED AVLAVAETFR
GRGRKTRRLE VSHAFHSPRM DLMLDAFRSV AETLTYVAPR IPVVSNASGR LATSGGLVSA
DYWVRHVRQA VRFGEGVACL AEQGVSVFLE LGPDGVLSAM GAESVADGVF VPVLRSGRAE
AESLLSGLAQ AWVRGVAVRW AEVFAGTGAS RVDLPTYAFQ RERYWLDTSS SADDTAAASA
LGLGSAGHPL LGAAVELPDS AGVVFTGRLS LRSHGWLADH AVGDTVLLPG TGFVELAVRA
GDEVGCDVVE ELTLEAPLVL PERAGMQLRL TVDEPDEAGR RALNIYSRPE DTGFDAAWTR
HATGTLAEGA TEPASDLTVW PPEGAQALDT AALYEDFAAA GYDYGPAFRG LRAAWRRGEE
IFAEAALAHE QQTEAARFAM HPALLDAALH GLRLGEFFGG PDTVRLPFSW AGVALRAAGA
SVLRVAIKPA GQDAVSVAVA DGTGTPVASL ASLVLRPVDP AQLGAARSGP LDDSLFRVDW
TALPHPRQTS GPWAVVGPDE FKLSVELGGE AEVAVHTDLA ALADAIGAGA PLPEAVFVAC
VADRGPAEAG LTTVPSDART TLGNALALLR SWVADERFAA TRLVFLTRGA VATRSSDELI
DLVNAPLWGL IRSAQSEHPG RFLAVDLDED ETSCRALPAA VATGEPQLAV RGRDLLIPRL
ARATTAANDP GLVLDPSGTV LVTGATGTLG GLVARHLVTE HGVRRLLLTS RHGPAAEGAA
DLHTALTALG ADVTIAACDT ADREQLARVL AAVPTEHPLK AVVHVAGVLD DGVIDTLTAE
RVDRVLRPKL DAALNLHELT LDLDLDAFIL FSGAAGAFGT AGQGNYAAAN VFLDALAHHR
RARGLPAVAL GWGLWSERSS MTERLDDSGV KRLARMGIAP MSSAHGLALF DAVAGADGAA
VLPVRLDLAA LRSRTSAQDV PPLLRGLVKP AVRRAASGGT TAADAVGAAS LRDRLSGLED
TEQDRVLLDL VRGHVAGVLG HARPEGAHAD RSFKELGFDS LTAVELRNLL NEATGLRLPA
TLVFDYPTPA ALAEFIKAEI GPARQAGPMA VLREIDALEA ALAASDTLTE PVQARLQELL
SQYGIRAGDS AGGPAEESVT DQLEAASDDD LFSFIDEHL
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