UniProt: A1U9G3

Database: UniProt
Entry: A1U9G3_MYCSK

LinkDB:  A1U9G3_MYCSK 
Original site:  A1U9G3_MYCSK

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Ontology (4)   
   GO (4)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (42)   
   InterPro (22)   
   Pfam (9)   
   PROSITE (4)   
   SMART (7)   
All databases (48)   

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ID   A1U9G3_MYCSK            Unreviewed;      3693 AA.
AC   A1U9G3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ABL89471.1};
GN   OrderedLocusNames=Mkms_0254 {ECO:0000313|EMBL:ABL89471.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL89471.1};
RN   [1] {ECO:0000313|EMBL:ABL89471.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL89471.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000518; ABL89471.1; -; Genomic_DNA.
DR   STRING; 189918.Mkms_0254; -.
DR   KEGG; mkm:Mkms_0254; -.
DR   HOGENOM; CLU_000022_35_8_11; -.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08952; KR_1_SDR_x; 1.
DR   CDD; cd08955; KR_2_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; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; 4.
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; 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; IPR006162; Ppantetheine_attach_site.
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; 2.
DR   Pfam; PF13602; ADH_zinc_N_2; 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; 2.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 2.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 2.
DR   SMART; SM00825; PKS_KS; 2.
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; 2.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 5.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
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   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          29..455
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1496..1570
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1594..2019
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          3595..3673
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3693 AA;  394219 MW;  76FDE968D4578366 CRC64;
     MSHRGRALTA DAREDTNGME SAAYPHVPAN RFAIVGYAAR FPGAQDADEF WDLLRDGREA
     ISEVPQDRWN VDEFFDPEPG APGKVVTRRA GFVDDVTGFD APFFGMSTRE VRLMDPQHRL
     LLETAWRAVE HSGTAPTDLA NSNTGVFVGL ATHDYLGMAS DELSYPEIEA YMAIGTSNAA
     AAGRISYRLG LQGPAVAVDT ACSSSLVAIH QACQALQLGE CDLALAGGAN VLLTPATMIT
     FSNAHMLAPD GRCKTFDAAA DGYVRGEGCG VIVIKRLEDA LRDGDRIRAV IRGSAINQDG
     ASGGLTVPNG VAQQRVITDA LKRAGVRAGD VGYLEAHGTG TSLGDPIEAQ AAGEVLGAGR
     EPSRPLLIGS AKTNIGHLEA AAGIAGVIKV ILSLEHETLP KHLNFTTPSP HIPWDRLAVK
     VVTESTPWER NGRPRIAGVS SFGFAGTNAH VILEEAPEST VTPAATPEPG ERFSLLPLSA
     RTPAALVRIA DRYRSWMTTH PEATLADVCF TASTARAHLE QRAALVVDSR ESAVELLGAL
     ADDRPAPGLV RGESHDTPKT AWLFTGQGSQ YPGMARELFD TEPVFAETMK QCAAAVADVL
     EKPLLDVIFD AHGPEAAETL RQTSYAQPAL FAVEMGLARL WQSWGFEPDV VLGHSVGQYA
     AACVAGVLGL EDGARLMAER GRLFGSLPAG GRMVAVFTAA ERVENITDEY PRLSVAAYNG
     ANTVLSGPAG DLEKAVATLA ADGIRCDWLD TSHAFHSALL DPILDEFESY AQQIEYAAPQ
     RVLIDNRTGA ALGWSAKLDG TYWRRHARQP VEFAKSVRTL AELNCKVLLE IGPRPVLTAA
     ALSAWPDPAT APRAIASLRR NTADHRQITE ALADAYVLGH RPDFAAIQRP DAHKLDLPTY
     PFEHRQYSFR DNQAERPEQA GPPIHQAART EAVGLLEDGR IEELAALLGD TDGDRQTFDV
     LSKLAAQHNQ QRTSQSITDD RYEIRWEELT TASPAATGEP STWIIVGDDT DAARPLIDAV
     TARGDRHRLV GSPVSDADEA SLADALRASV DDASAPGGAV RILHIAALDA TTAPSMRTLL
     SMQHRILGRT RRLFHAVTTT GLRTPIWLIT RGAQRVTATD TVAPDQSALW GFGRAASLEL
     PHLWGGLADL PTGPGASEDE WSRLLDRIAA PRHSDVTEDQ VALRDGAVHV PRLVRRTGQP
     SGAPLRLRSD ATYLVTGGLG AIGLEIAGYL AAHGAGNIVL TSRRAPGDAA QQRIDALRDK
     FGCAIRVATA DVADAHDVAR LLAGVQAELP PLAGIVHAAG EIGTTALSAM DDESQQAEVD
     RVFAGKVWGA WHLSEAAVDL QLDFFISTSS IASVWGGFGQ TAYGAANAFL DGLAWRLREQ
     GIAATSVNFG PWSAGMADAE SRARLEQRGV RTLDPADALA GLADVVAGPA TQGVIARIDW
     ARFLPLYQQA GRRAFLTELE REAPVASTDA APAVTASGKT PLVERLSGAP VQQRKKLLTD
     YLRDAVAEVT RVDSAEIRED AGFFDLGMDS LMAVELRRRL EQGVGKEIPV TLVMDHPRLS
     DAADYLLGEV LGLAEQAPAE SRPALASLAS ERTDDPIAIV AVSCRFPGAP DPEAFWDLLS
     GGVDAIREVP EDRFDIDEFY DPDPDAAGKT YTRFGGFLDG IDGFDPEFFG ISPREAVWIE
     PQQRLMLETV WEGIERAGLS PADLRGSRTG VFVGVAANEY AHLLSSESIE KIEPHFITGN
     ALNAISGRVA FALGLEGPAV AVDTACSSAL VAVHQAVQAL HSGDCDLAVA GGVNVLLSPV
     TVVAASRARM LSPVGRCKTF DASADGYVRS EGCGILVLKR LSDAVRDGDR VCAVIPGTAV
     NQDGASSGLT VPNGGAQQRL IKTALTRAGL TGGDVDYLEA HGTGTPLGDP IEVQAAAAAY
     GASRDADRPL LMGSVKSNIG HLESASGAAG LIKVVLSLQH GVLPQSLHFD NPSPHIPWDS
     LPVRVVDEAV PWQPNGRPRR AGVSSFGFTG TNAHVLVEEA PQAPVSEDQE SDTDDQPVHV
     LPLSARSPEA LVALARRYDS WLGAHPDADL AGVCFTAGTG RSHFEHRAAM VVDSVASARQ
     GLADLADNRT RPGVVRGEHT NRPTTAWLFT GQGSQYPRMA RELFDAEPVF AETVTRCADA
     VDGMLPLPLL EVLFAADRET AERLRHTSYA QPALFAVEMG LARLWQSWGV TPDVVLGHSV
     GQYAAACVAG VFSLEDGARL MAERGRMFGS LPEGGRMVAI FADAKQVEQI AGEFARVSVG
     AYNGPNTVLS GPGEDLEQIV ARFADEGIRC TWLETSHAFH SELLDPVLDE FESYAAQFEF
     AAPTMPVVCN RTGAVLTGQT PLDAQYWRRH SRQPVQFAES VRTVATLGCS VLMEIGPQPV
     LTGAAVQIWP EHLAAPRAIA SLRKGVGDRR QIADALAAAY VGGLRPDFAA LQGQPHHRLE
     LPTYPFQRRR FWPKTSSITV DGPATSGILG SAKDLASGDT VYTSRLSVKS QPWLSDHVIY
     GTVVVPGATY AAMALAAVGT PARVKDVFFY EPIILPEKSS REVQLTLHIL GDGEQKFQVH
     SRSYGVRDAE WSLNAEGTVV RGVDDAPVSQ DDPVDEAIER CNRMRPQELF ETFADMELAW
     GPTWSGSLKS LWLGDGEAIG DVLVGAELAE QLGSEPIHPV LMDLCTGVAF PAFPALLAAE
     QGVSDLFLPL RYGQVTVQEK MPRRFYCRAK WHHSELDSET QVFDLDFISR DGRPLGGIRE
     FTVKRAPREA LLRGLGGDAT RLLYTLGWHE VPLPAVDPAA PNGNWLIAGF DELAASVPGC
     IPFDRTTDPE PLGQLLTQAH ERGMAFSGVV WRAAAPKPDE SSADVAARIE TEIANLLSAV
     HAVQRGEVKL PGGLWIVTER AVACESGEPV DPVQAALWGF GRTTINEEPA LRCKLVDCDG
     SPEAVEALSA LLTTPVDEPE LALRQGKLLA SRLLHWARSG HLTVPRSTDY VLAPTERGAI
     DNLRLTETEV PPPAEGYVQV EVEAAGLNFR DVLNVLGLYP GDPGPIGGDF AGVVTQLGDG
     VGSGRAERRD GIKLEVGQRV YGFMQGAFSS RFNVPAQLLA PIPDGVGAVE AATIPAAALT
     ARLAFDWAQL EPGDRVLIHA ASGGVGLAAI QLAQQHGAVV FATASTYKRA TLRKMGVEYV
     YDSRSTDFAD QILADTDGAG VDVVLNSLTN EGFVEATVRA TAQNGRFAEI AKRDIWTHEQ
     MAAARPDISY EIVALDTVTI QEPERIRGLL GEVSDGLGKG EWAPLPAEIY PLTEARAAFR
     RMQQARHIGK IVVQMPSPLQ PRPDRSYLIT GGLGAIGLHT ASYLAQLGAG DIVLTSRREP
     DADTQQVIDE ITDRHRCRIH TFAADVGDES QVEELLERIR AELPPLAGVA HLAGVLDDAL
     LSQQSVERFR TTLAPKAFGA YHLDHLTRDD DLDFFIVSSS VSSLFGSPGQ ANYATANALL
     DGLVARRRAH GLPATGVNFG PWAQGGMASS EAATANISAQ GLVPLEPSAA LSALAEVVAN
     GTAQATVIKA NWQRAAKVLG ASRPPLLDLV LPSAAGEVTG DSELLRQLQE IPVAQRAGFV
     TEFLQREVQN FLRLAQPPAA SSRFLDLGTD SLMAIELRNR LHSQFGGAFT INATAVFDYP
     TIGGLAEYLV GQLPDAESPA AETAPAAEVP AAD
//

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