UniProt: M3C0Y2

Database: UniProt
Entry: M3C0Y2_STRMB

LinkDB:  M3C0Y2_STRMB 
Original site:  M3C0Y2_STRMB

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Ontology (4)   
   GO (4)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (40)   
   InterPro (21)   
   Pfam (9)   
   PROSITE (4)   
   SMART (6)   
Literature (1)   
   PubMed (1)   
All databases (47)   

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ID   M3C0Y2_STRMB            Unreviewed;      1900 AA.
AC   M3C0Y2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:EME97616.1};
GN   ORFNames=H340_25542 {ECO:0000313|EMBL:EME97616.1};
OS   Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1223523 {ECO:0000313|EMBL:EME97616.1, ECO:0000313|Proteomes:UP000011740};
RN   [1] {ECO:0000313|EMBL:EME97616.1, ECO:0000313|Proteomes:UP000011740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40847 {ECO:0000313|EMBL:EME97616.1,
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   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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:EME97616.1}.
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DR   EMBL; AORZ01000110; EME97616.1; -; Genomic_DNA.
DR   RefSeq; WP_004951565.1; NZ_CP072827.1.
DR   STRING; 1223523.H340_25542; -.
DR   PATRIC; fig|1223523.3.peg.5184; -.
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: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; 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; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; 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; IPR015083; Polyketide_synth_docking.
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; PF08990; Docking; 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; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 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; 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          34..460
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1742..1817
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1900 AA;  197105 MW;  ED060C439587E19F CRC64;
     MAATYEKVLE ALRASVKEAT RLKQENQRLA DAAREPVAIV GMACRFPGDV RSPEDFWRLL
     ADGTDAVGPF PEDRGWDTDE LYDPDPDRVG KSYVRHGAFV RDADRFDAAF FGISPREAVA
     MDPQQRLLLE TAWEAFERAG IDPESVRGSR TGVFVGTAPL GYATGARQGS DGAEGYLLTG
     TTVSVASGRL AYVLGLEGPA VTVDTACSSS LVALHLACQS LRRGESTLAL AGGMAVMAEP
     RMFVEFSRQR GLAPDGRCKA FAAGADGTAW GEGGGVLLLE RLSDARRNGH PVLAVVRGSA
     VNQDGASNGL TAPSGPSQQR VVREALADAG LTPDQVDAVE AHGTGTSLGD PIEAQALLAT
     YGQGRPADRP LWLGSVKSNI GHTQLAAGVA GVIKTVLAMR HGTLPRTLHV DAPTPHVDWS
     SGAVSLLTEP VDWPETGRPR RAAVSSFGIS GTNAHVVLEQ GDGPSSAEEL PDGEGPLLWA
     VSARSPEALR AQAARLADAV RTHPDWRPGD LARVLVRSRA ALEHRATVTG TTRDDLLTGL
     DALRDGVSAP RLVRDTVRRA GKTAFLFTGQ GAQRAGAGAE LHAGHPAFAR ALDDVCEALG
     DGLGAETRAL VLGTGDPALL KGTLHAQTTL FALETALFRL LEAWELRPDA LLGHSIGELA
     AAHAAGVFSL EDAATVVAAR GRLMARLPSG GGMTAVQADE EEVLPLLADR AHLAAVAAVN
     GPRAVVVSGD EDTVREIAGR FAADGRRTKR LDVSHAFHSP RMDGMLDGFR AVLDRVTLHA
     PALPLVSDLT GRTLTADEAR DPGYWVRHVR DTIRFRDGVR RLLAQGVRTC LELGPAGVLS
     ALAQDTAAED GGDLTAVPLL RRDRPEPETV RTAFAHAWAR GARTGLAAAL PAGPTPHLDL
     PTYAFQGERH WLRPADAGDG PAGPAALGLD AAGHPLLTAA VRPADDDRLV LTGRISTRSH
     PWIADHVVLG TVIVPGTAYL DLVLDAARRV GCGTVEELNQ EAPLILTGTR PADVQLTVGA
     PDADGRRAVA VHSRPDDGAE WTRHAHGTVA PGTPEPARDL SGDWLPADAV PVDLTDFYPS
     VVADGFAYGP TFRGLTALWR SGDEVFGEVA LPEAARTDAA GYGVHPALLD AALHAGLVGN
     TGDTVRLPFC WNRVGLHTTG ATALRVHLAP AGPDAMRLTV ADADGTPVLT ADSLQARPVS
     LGQLQAARRD ETLHELRWTA APDAEPETRA RTWALLGDGV PGLPGALPAG DRLVGYEAGA
     GVPGAAPVVP APGRRAGDAA AEVLPADDRL VADAADAGVP GPAPGLSIGG AAAETLPADD
     PLLGAAGVPD VALVAPAPGR PVRETVAETL DLLQRWLADE RTASSVLAVL TRGAVATGPG
     ESVPHPELAA VWGLVGAAQA ENPGRFVLAD LPPDTDATPE LLTALLAGEP QLALRDGAVR
     VLRLAPARLP ADAVPPVLGP DGTVLVTGGT GALGALVARH LVERHGVRHL LLLGRQGPAA
     EGAGELVTDL KERGAHVDVR ACDVSDRTAL AAALAAVPAD RPLTAVVHAA GVVDDAVVPA
     LTAERAAAVL APKADAAHHL HELTRDLPLA AFVLFSSATA TLGGAGQGSY AAANAYLDAL
     AAHRAAAGLP ALSLAWGPWE GTGGMADALD EAGRRRMRRS GVLPLSADEG LALFDAALAA
     DRPVLLPVRL ETAALRAASA QLPPLFHGLV PPPAQAVRAA GPDAAGDLRR RLAGLDAAGR
     DRVLLDLVRT QAAQVLGHAG AAAVAPDQPF EDLGFDSLTA VELRNRLTAA TGTRLSATLV
     FDYPTAAALA RHLREALPDG DAPAARSVLD DLDRLEAALA ALPADDPDRV RVATRLRAVA
     ARWDDDRPVP ADDEPASGTD LSAADDDEVF DYIEKELGIS
//

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