ID M3BYB1_STRMB Unreviewed; 2506 AA.
AC M3BYB1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Putative type I polyketide synthase WcbR {ECO:0000313|EMBL:EME96750.1};
GN ORFNames=H340_29956 {ECO:0000313|EMBL:EME96750.1};
OS Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1223523 {ECO:0000313|EMBL:EME96750.1, ECO:0000313|Proteomes:UP000011740};
RN [1] {ECO:0000313|EMBL:EME96750.1, ECO:0000313|Proteomes:UP000011740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40847 {ECO:0000313|EMBL:EME96750.1,
RC ECO:0000313|Proteomes:UP000011740};
RX PubMed=23558536;
RA Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT Transglutaminase.";
RL Genome Announc. 1:E0014313-E0014313(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EME96750.1}.
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DR EMBL; AORZ01000177; EME96750.1; -; Genomic_DNA.
DR RefSeq; WP_004954611.1; NZ_CP072827.1.
DR STRING; 1223523.H340_29956; -.
DR PATRIC; fig|1223523.3.peg.6083; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR Proteomes; UP000011740; Unassembled WGS sequence.
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: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; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
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; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR013149; ADH-like_C.
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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..435
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2368..2446
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2506 AA; 262201 MW; CD12C49BA926E937 CRC64;
MEADGREGAG RDPGAAIAIV GASCRLPGGI GGLAELWAAL EEERDMITTL PPGRFDPVRF
VDTGHPRPGK SYTAAGGFLE DPAGFDAAYF GISPKEATAM DPQHRLLLEL TAEALDDAAV
DPARLAGTDT AVFVGISDGS YAVMPAPREV TPYTMVGGAL ALAANRVSHA FDLRGPSMSV
DTACSSALVA LDRACRALRD GSCRTALCGG VNILLNPQQF VGFSQASMLS ARGRCAAFSA
HADGFVRAEG GGVVLLKPLA DALADGDRVH GVILGTGTNC DGHTPGVFLP STEAQEELLR
RTAAEAGVDP DELVYFEAHG TGTHVGDPVE ATAIGRALGM RRITGDLPIG SVKSNLGHLE
PASGMAGLCK ALLVLRHRTV PASLHAEPLN PAIDFAGLGL RPATGKLPVT ASGRAVVGVN
SFGFGGANAH VLVAAPDPAP EPDPAPPARP LPVLVSARSA RALREAAARL ADRLDACPER
EFPDAAGTLW RRGRHEHRAV VLATGAREAA RALRALTADG PAPDAPEGAV GKAAGRGRVA
FVYSGNGSQW PGMGADLYAR EAVFRDAVDE LDARLAPRLG WSVAEALTRP PGSWRLEATE
CAQPLLLAVQ LGTTAVLRAH GITPSAVLGH SVGEVAAAHA AGVLDTEGAA RVIAERSAVQ
APTRGAGRMA AVGLSAEEAA DVLARYGDTV VLAGINSPRD VTVAGPAPDL AALGERLRGR
GVLFHELDLD YAFHSPAMDG CEAPLTRALD GLEPSPATVP FYSTVTGTQL LGTELDAHYW
WHNIRRPVRF ADAAALAHED GADVLLELGP HPVLTGYLRR STRGDRRKPV TVLPTLRRAD
AGPRVLATTV AALIAAGAGA SGPAFRPGRV VDLPAYPWQR GRHWTGGPRS WLRDPGDGVL
DHPLLGERVP APHPQWHGPV EPVAAPWLPD HRVKGAVLLP ATGYVEMALA AGRRTLGDGP
LDVGRLLIRS GLVIPRDDPG ALALQSSLRP DDGTMTITST ARPGDTPRVH ATARVRTLTA
PRPAPVDPAA VRARCPRHVR AADYYRDRAA TGLEYGPAFQ VLTELSAGPA EVLAAYRHDA
PGAPYVVHPA LLDGALQAGV QLLADRLDAG QAFLPASIAA VRVWDTPSAT GFVRARELFR
SEDEVRWDLS LTDPDGRVTV HVEGCRLRRT SVGGGTPVTV HHTALRAAPR PGRPGSPAPL
PPPRRILDAL RPPEPPLRPG DERRARDALD EFAARHHANA LARLLPDARA PFAVTDLLGP
EPSAGHRAWA LRLLDLMCRH GTALPLGDGR HRLTADNHDT AAPAHRCLDA APAFGTALAL
AAAADRYWTA APDAPPADHT ETAELVQETL PAERRRCRLL RAALSRVAEL WPAERPLRVL
DTGEGATAVA LLPVLPPDRT HYRLTGVPPA ARPALLARLA ALGHDAVVEL TDPLADEAGE
DFDIVLDDTP GDRPDPEAAL RRTAALLTPG GYLITSLAHD TALRDLLHGP ADGPALRPPP
DGDAWPDLLR RAGFTDVARA DTDGHTVLLG AAPSTPRRPE QPLATPPDAA FLLVTADRRE
DGLVTALAAA LTRPGAPAVA TGRAGGTAEE WTALLDAVPA DDAATRHVVL LVGRTAGTGP
DAPTAHAART IAALGALAAA HARRDSGPGT RLWLVTHPHD ALPGPVRDAD PAAAALWGAA
RTLANEHPRL DTRRIALSRT GDPAADAERL ARELVAPDEE DEVVLTPEGR FVPRERPGTA
PVRMRPGETA FRLRLRDPGL SYRLSWTETV PARPGPGEVA VAVRAVGLNY RDVMQVMGLL
PGELTEGTPS ERGPGIECAG TVTACGPGVT QFRPGDRVVG VAPSCLATHT VTPVHWLTRL
PDGIAFTEGA GAPIALITAH YGLGHLARLR PGETLLVHGA AGAVGLAALR YARHHGAHPI
ATAGSGLKRS ALRSLGMEHV LDSRAPDFAD RVRALTGGRG VDVVLNSLAG EAVVRGLELL
RPGGRFVELG KRDIHENKPL PLHPFDNNIA FFGLDISALL PDRAFCARLI DEALIAELGH
GTYHGLPHTT FPAARVHEAF RLLRHSRHIG KVVVTFEPDD EPPPVEPAAS PHRPDPNGTY
LVTGGTGGFG AVTARRLADR GARHIALVSR RGAAAPEAAA VLAALAARGV RATAYAADVT
SAKAMRSVVR KIDRTGFPLR GVVHAATRYD DAPLTELDEA GAAAVLAPKA TGAAVLDGLT
RDRECDLFLC HSSGTALLGN VHQAPYVAGN LAVEALVRRR RREGLPGLAV AWGALSDTGH
AARDGLLDGL AAVGVEPLTS RRALAVAEGL PATTDVVGAG RYHWPRVAAL LPQATRPRLG
ALVPAGAADD GTARERRLDA LRRMPAEAAL DLLVEELTRL VADALGTSPD GLDPHTRLDA
YGMDSLTGTQ FFATLQQTYD VRIPPMELLS GNGTITGVAH QLRLGLGLEG KGGGDDAGER
DGTGSRDGHD GRDGQDGRDG RDGHGGHGGH DGHSGHDERP AGTQEA
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