ID B1LZR4_METRJ Unreviewed; 2485 AA.
AC B1LZR4;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ACB22962.1};
GN OrderedLocusNames=Mrad2831_0952 {ECO:0000313|EMBL:ACB22962.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB22962.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB22962.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001001; ACB22962.1; -; Genomic_DNA.
DR STRING; 426355.Mrad2831_0952; -.
DR KEGG; mrd:Mrad2831_0952; -.
DR PATRIC; fig|426355.14.peg.991; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_31_5_5; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000006589; Chromosome.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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; 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; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
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 9..431
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2361..2438
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2485 AA; 263024 MW; F62A57FF43CA7688 CRC64;
MCEPNVTQRT DIAIVGRACR LPGAPSVDGL WSLLSEGRCA VSKVPADRFS LERFAHPRAH
ERGKSYTWAA GVIDDVWSFD PAVFGISPRE AEQMDPQQRM LLELTWEALE DAGLRPSSVA
GSNIGVFVGA SSLDYGNLRI LDAPSGDAYA ATGNTLSIIS NRISYIFDLK GPSFTVDTAC
SSSLVAFDNA VQAIRSGRVD TAVVAGVNVL ASPFNFICFS TAQMLSRTGL CQAFSKNADG
YVRSEGGVVF VLQSAEAARR NGATVRAVVA ASGINSDGRT TGISLPSGYA QGALLEKVYR
EAEIRLDDLA FMEAHGTGTP VGDPIEASAI GSKLGRGRQA PLPIGSIKTN IGHTEPVSGL
AGLMKATLAL EHDLVPPSLH AAELNPEIPF GELNLHVVRE AMPISRGARE RFAGVNSFGF
GGTNAHVVIT DAPAWAKPAA ATAEPQAQVL LLSAQSRAAL NELALDYAER LESAPEQVAT
VAAAVAHRRE RMPARLAVAL DGKADVAAAL RAVGEGEDTP DAFTGTAVDR VAEVAFIYSG
NGSQWAGMGR EAYEENAVFR ATFDRIDTLF RAYSDWSLKD ALYADDLDER LALTSVSQPL
IFAIESASTA ALKAKGLIPS YVLGHSVGEI AAAEAAGILS LEDAVRVIYY RSHHQETTHG
QGTMAVLLMP SEEVETFLKD YPTLDIAAYN SPKAVTVAGP VADIDAALKA LSRKRRRGRK
LDLAYAFHGR LMDPTEKPLL RDLAGLKAKA GTTAMVSTVT GSVLDGSHFG AGYWWRNIRE
PVRFCEAVQD ATRRGARVFV EVGPRATLMS HVGDAVEPLG IETATVGVMH RKASGGDPIA
KAVSAALVQG AQVDETLLFG DAPKGDVRLP TYPWQRRPFR LADTTEGVGA MSPRPYHPLI
GSRTAFDGLE WNGFVDPVTV PELEDHKVDG QVIMPGAGFV EMALACVREA LRDDAVVLAD
FEIVAPMVFA EDALREVAVR LSGSGNGIQV LSRPRLTQTP WQLHAQAKIV EGSFSAPKAP
DLDGFSFETA GDHVLTGDAL YAKALASGLG FGPSFQQVAM SARLDDATIV SDLLPAEPDT
RYGLVPNRLD ACFHGLILLF ADLLGENGGK AYIPVRFGEV RLLRPGAVIA RSIIRTRRCN
ERSILADFTL LDAEGAVIAT IREGRFQALR AKSGGDLSAF AISQVPELAT EPTAIPMERR
PSVAARLRPL AAEAKGPADA ALSPGHLLLE GWATSLAYRL ASGLAQGETV TVTDSRVPEA
LRPWLLNALY ALESSGLAER AGPNWTLGDG SALPAPDEIM RWIAGDHPDL SAELVLIADV
GALVDRLLAG TLSDAPALPQ GAIDAFVLRS ATARHGADVV ADLIERSRAQ LPKERALRVL
QVGFGPLSAQ TATFAAAAEA RLTVFETDRR LAERARLSLG RAAAVVETAE ELAPGSFDLI
LASGSLHRGD RALPGQLAGA LATGGLLVAV EPGASLFRDL VFGLTAGWFE EAAGGLPVGR
LEDIEGWQRI LSAHGLVKVE VERAASANGD DLLLTAEAPV RPGPAPAQSF AFIIGSDDEF
AAETASSLAT LLVAGGVHVS IILDSETSLM ELEKETPDTV VFLAGAFTRG GEAAERLRDR
CLSLKRCTEH LGSRQTRLWV VAPGATRDRG GQTTNIEAGV WAFSRTLANE APNLDVRRID
LSPEMSSKRA SERLRDLILS GTPETEIVLD DERTQVVRFH AGRPQHRDPA DAVPAEAARL
ERSNTGGLSE MVWGPAERRA PGKGEMEIAV EATGLNFRDV LWALSMLPEE ILEDGFAGPR
LGLECAGRVT AVGPGVKGFK VGDPVVAFAQ SGFATHIVVP DLVVAPMPQG LDPMAAATVP
VAFLTAYYGL VSCARMRRGE WVLVHGGAGG VGLAALQIAK LKGARVIATA GSREKRALVK
ALGAEHVLDS RSLAFVDEVR AITGDGVDIV LNSLFGEAME RSLNALRPFG RFVELGKRDY
VANTHIGLRP FRRNLSYFGV DLDQVIQHQG DDGARMFREV MALFNDGGLK PLPYQPFTAA
ETSDAFRLMQ QSGHIGKIVI SPPKAGTIMK DTARPFTVSA EGVHLLTGGL GGFGLEAARW
LIDRGAKHLV LAGRKGAATD EAKAIVAELT ARGVTVEAKA VDITSRASVD RLIAGIEQGG
KKLAGVLHAA AVLQDGLISN IDAAALDAVI GPKVIGAQHL DAATRDRSLD YFVLFSSATT
FIGNPGQGSY VAANGFMEGL ARQRRRRGLP ALAVAWGAIG DVGMLARNKA VMEGLAGRVG
VTPMEARRCL DLMAEALGSQ GASPDEGVIA IAAMHWGKAR ERLATMRSPS YAELGSDQQA
EAGGVQAINI AALLKGGDLD AVRKTVSDAI VEDIARILRL PKDDISRVRQ LSEIGLDSLM
GVELGASLQE RFALDAPPAG LSSGMTVNEL SESLIQAVSA PMDETAGVAM SLVSKHVGGE
VDAQILAPLK ELIEQTSSEI KETNS
//