ID D1YVP6_METPS Unreviewed; 464 AA.
AC D1YVP6;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Putative pyruvate carboxyltransferase {ECO:0000313|EMBL:BAI60518.1};
GN OrderedLocusNames=MCP_0446 {ECO:0000313|EMBL:BAI60518.1};
OS Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS SANAE).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60518.1, ECO:0000313|Proteomes:UP000001882};
RN [1] {ECO:0000313|Proteomes:UP000001882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC {ECO:0000313|Proteomes:UP000001882};
RX PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA Mori K., Fujita N., Imachi H., Takai K.;
RT "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT paludicola, the first cultivated representative of the order
RT Methanocellales.";
RL PLoS ONE 6:E22898-E22898(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA +
CC H(+); Xref=Rhea:RHEA:12929, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58884; EC=2.3.3.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000523};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930;
CC Evidence={ECO:0000256|ARBA:ARBA00000523};
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154}.
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DR EMBL; AP011532; BAI60518.1; -; Genomic_DNA.
DR AlphaFoldDB; D1YVP6; -.
DR STRING; 304371.MCP_0446; -.
DR KEGG; mpd:MCP_0446; -.
DR eggNOG; arCOG02093; Archaea.
DR InParanoid; D1YVP6; -.
DR Proteomes; UP000001882; Chromosome.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42880; HOMOCITRATE SYNTHASE; 1.
DR PANTHER; PTHR42880:SF1; ISOPROPYLMALATE_HOMOCITRATE_CITRAMALATE SYNTHASE FAMILY PROTEIN; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:BAI60518.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAI60518.1}.
FT DOMAIN 19..279
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 464 AA; 52941 MW; D6B11B2DCD0DF9FD CRC64;
MMRRYDEMPK IKLPNAKDIK ISDTTIRDGC QMPGIVMKKS HKLKIFEYLH DMGVEKLETF
IYNDRDKDAA RAMMDYSYDF PEVTGWARAN PADIDEVLKV GGIRETGILM SISDSHIYDK
MGLKSYEEAE KKYLNALQYA VDHGLKTRCH IEDTSRANYA FVYPFIRKCI EIDPHTIIRV
CDTLGYGVPF PEEEEPYGIP IVVKKLKEIG VKHIEMHVHD DFGLGVANTL AGLWYGADWA
NLTFLGIGER AGNSELEKIM AFLITRVEGF DKYDLRTVTE FAQYMEDEVG LRVPRNKAIV
GKNIFSHESG IHTAGIIKNP FTYEPFPPEL VGGKRNLMIG QTSGTEVVRL KAEEALNELL
GIEVHVEKSD SRIKSIHNEI QKMYDAEERR SSVSDEEMKD YVRKYFLYQV DGWEEELEER
KAKKKLNLTL VNPEFMPLDG IPAAATSLTD KSVKKVKNGS SKKK
//
