UniProt: M3AT66

Database: UniProt
Entry: M3AT66_STRMB

LinkDB:  M3AT66_STRMB 
Original site:  M3AT66_STRMB

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Ontology (4)   
   GO (4)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (41)   
   InterPro (22)   
   Pfam (9)   
   PROSITE (4)   
   SMART (6)   
Literature (1)   
   PubMed (1)   
All databases (48)   

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ID   M3AT66_STRMB            Unreviewed;      2896 AA.
AC   M3AT66;
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:EME96787.1};
DE   Flags: Fragment;
GN   ORFNames=H340_29756 {ECO:0000313|EMBL:EME96787.1};
OS   Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1223523 {ECO:0000313|EMBL:EME96787.1, ECO:0000313|Proteomes:UP000011740};
RN   [1] {ECO:0000313|EMBL:EME96787.1, ECO:0000313|Proteomes:UP000011740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40847 {ECO:0000313|EMBL:EME96787.1,
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:EME96787.1}.
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DR   EMBL; AORZ01000172; EME96787.1; -; Genomic_DNA.
DR   RefSeq; WP_004954442.1; NZ_AORZ01000172.1.
DR   STRING; 1223523.H340_29756; -.
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; 2.
DR   Gene3D; 3.30.70.3290; -; 2.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; 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; 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; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR   Pfam; PF00698; Acyl_transf_1; 2.
DR   Pfam; PF08990; Docking; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 2.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 2.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 2.
DR   SMART; SM00827; PKS_AT; 2.
DR   SMART; SM00826; PKS_DH; 2.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS50075; CARRIER; 1.
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          33..457
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1738..1813
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1834..2261
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          1436..1456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         2896
FT                   /evidence="ECO:0000313|EMBL:EME96787.1"
SQ   SEQUENCE   2896 AA;  301448 MW;  AD1FE0219A8B54A0 CRC64;
     MASEEQLVDY LKRVAAELHD TRQRLREVEE RSQEPVAIVG MACRFPGGVA SPEALWELVA
     AGEDAIEGFP TNRGWDLEGL YHPDPDHPGT CYVREGGFLD GADRFDSGFF GFSPREALAS
     SPQLRLLLET SWEVLERAGI DPTTLKGSST GVYVGAATTG NPTQGDPAGK ATEGYAGSAP
     SVLSGRVSFT LGLEGPAVTV ETACSSSLVA MHLAAQALRQ GECDLALAGG VTVMSTPEVF
     TGFSRQRGLA PDGRCKPFAA AADGTGWGEG AGLILLERLS DARRNGHKVL AVLRGSAVNQ
     DGASNGFTAP NGPSQRRVIR QALAGANLST SEIDAVEAHG TGTKLGDPIE AEALIATYGK
     ERDEDRPLWL GSVKSNIGHT QAAAGVAGVI KMVMALRREL LPATLHVDEP TPHVQWEGGG
     VRLLTEPVPW SRSERVRRAG VSSFGISGTN AHVILEEAPA EVSDEVAPEP VPGAVVPWVV
     SGRTGEALRE QARRLGAVAS ENSSPLDVGW SLATSRAAFE HRAVVVGQDV GQALAGLEAL
     AAGEASPDVV SGVAGDVGPG PVLVFPGQGS QWAGMGAQLL DESPVFAARI AECERALSPY
     VDWSLTEVLR GNGDALSRVE VVQPVLWAVM VSLAVVWAEY GVKPAAVIGH SQGEMAAAVV
     AGALSLEDAA RVVAVRSDAL RRLAGRGAMA SLGVGRGVAE EFIDGHAGVG VAAVNGPSST
     VISGPPEQVA TVVAEVEARG YRARLIDVDY ASHGPQVDEI ADLLADRLSG IEPQATTDIA
     FYSTVTAGRI DTAALTSDYW ITNLRQQVRF AETVEALLAD GYRVFVEASP HPVLNLGMEE
     TIERADVAAT VVPTLRRDHG DALQLARSVA HAFTAGVDVD WRRFFPTDPS PRTVDLPTYA
     FQHQRYWLEV DGVGDVRQAG LRRLEHTLLP AALGLADGAL VLTGRLAASG AAGWLVDHAV
     TGTTLVPGAA LVEWALQAAD EAGCPTLEEL TLQAPLALPD SGGLQVQVVV GPADERDGRR
     EVRIFSRPDT EDAVDHDEAW ACHATGALSP ESASAADGEP GGAWPPADAE QVDIGGLYER
     ASAAGYHYGP AFQGLRTVWR HGEDLLAEVV LPDAAGAHDG FGIHPVLLDA ALHPALLLDE
     GPQEETEAGV RLPFAWNGVS LWATGATEAR VRLSPHRGDG DEPDLRLTVT DATGAPVLSV
     ASLAVRRADP EQLRAAGKAR AKGLFTVEWT DVPLVDVSSA GVGDGHGWAV LGQDAPAWAG
     TDLPRYETPA ALLESDAPVP GTVLVAPSPT PDTSTLAVEA HGHAVAERAL RLVQDWVAEP
     RLTDTRLVFL THRAAAVPAV DEPGDVDASA AALWGLVRSA QSEHPDRFVL LDVADGIDIG
     GGVHVTDGVH VTDGTDAAND EGLDRAAVAR ALASGEPQLA LRAGRVLAPR LVRATTTESG
     TGVDGSRRPG HSGLDPDGTV LIAGGTGMMG GLVAEHLVRT WSVRHLLLVG RQGPDAPGAG
     DLADRLTALG AQVRIVAADL TDRRAAEGLV ASIDPAHPLT GVIHAAGVLD DAVVTAQTPG
     QLARVWAAKA TVAANLDLAT RRADPALFVA FSSAAGVLGN AGQAGYAAAN AFVDALVTRR
     DGTHGTGTAL SIAWGLWARD SAMTRHLDET DLARLRAGGM KPLSDEQGLA LLDAARDVDG
     PAVVAAGIDV RGLAQDTAPA MLRKLAGPPR RRTAAGSTGD PAALETRLAG LDATERLAAV
     TELVRECVAA VLAYPTPADV RTEANFKDLG FDSLTAVQLR NSLTAASGLR LPATLVFDHP
     TPRALAAHLC TRLGGGPTAA PTAVPGVPAT VGTDDPIAIV AMACKYPGGV TSPEDLWKLV
     ESGVDTVGEF PTGRGWDLDR LFHPDPDHPG TSYADQGAFL HDAADFDAAF FGISPREALA
     MDPQQRLLLQ ASWEVLERAG IDPTSLKGTR TGTYVGVMYH DYAAGLASGE DPQLEGYSML
     AGSGSVVSGR VAYTLGLEGP AVTVDTACSS SLVSIHLAAQ ALRQGECDLA LAGGVTVMAT
     PEVFTGFSRQ RGLAPDGRCK PFAAAADGTG WGEGVGVLLL ERLSDARRRG HRVLGVVRGS
     AVNQDGASNG LTAPNGPSQE RVIRQALASG GLAASDVDVV EGHGTGTTLG DPIEAQALLA
     TYGQGRPVGR PLWLGSVKSN IGHTQAAAGV AGVIKMVMAM RRGVVPASLH VDVPTPHVDW
     ASGAVRVVSE AVSWPEVDRP RRAGVSSFGA SGTNAHVIIE HVPEPAEAVA RETDPVDDGP
     VPWVLSARSP EALRDQAHRL KEAVVAAPDV PARDVGWSLL RTRSLFEHRA VVTGTERVAA
     LGALAVGESH AGLVGPGVVR GGKAVWLFSG QGSQLVGMGS GLYERFPVFT EAFDEVCGLL
     EGELGGSLKE VVFSGPRERL DHTMWAQAGL FALQVGLARL WESVGIRPDV VIGHSVGEIA
     AAHVAGVFDL ADACRVVGAR ARLMGALPEG GAMCAVQATP EELADHLHGS GVSVAAVNTP
     DSTVISGPVD EVERIAAVWS AQGRKTKALS VSHAFHSALM EPMLQDFADA LAEVKFKSPA
     IPLISNVSGL PAGEEIASPD YWVRHVRQPV LFRQAVAHVA DEAGFFVELG PAPVLTTAAQ
     HTLDDVEGPE PLLVSSLGGG RPEEQAFLEA MARLHTAGGT VDWDIWFQGE GKPAVVDLPT
     YAFQRERFWL SGRSGRADAA GLGLVAAGHP LLGAAVEFAD RGGCLLTGRL SRSGVSWLAD
     HEVAGTVLVP GAALVEWVLR AGDEVGCATV EELMLQAPVV VPTASGLRVQ VVVDAAADDG
     RREVRVYSRP DDGDDAWVCH ATGILTPEPT AVPEGLIGAW PASGSVPVEV EGFYERMADA
     GYAYGPAFQG LRSVWR
//

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