ID A0B606_METTP Unreviewed; 353 AA.
AC A0B606;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Pyruvate carboxyltransferase {ECO:0000313|EMBL:ABK14130.1};
GN OrderedLocusNames=Mthe_0336 {ECO:0000313|EMBL:ABK14130.1};
OS Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS PT) (Methanosaeta thermophila).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=349307 {ECO:0000313|EMBL:ABK14130.1, ECO:0000313|Proteomes:UP000000674};
RN [1] {ECO:0000313|EMBL:ABK14130.1, ECO:0000313|Proteomes:UP000000674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT
RC {ECO:0000313|Proteomes:UP000000674};
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., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT "Complete sequence of Methanosaeta thermophila PT.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000477; ABK14130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0B606; -.
DR STRING; 349307.Mthe_0336; -.
DR KEGG; mtp:Mthe_0336; -.
DR HOGENOM; CLU_022158_5_0_2; -.
DR Proteomes; UP000000674; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
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; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:ABK14130.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000674};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABK14130.1}.
FT DOMAIN 1..207
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 353 AA; 40245 MW; 77975BD96B469881 CRC64;
MLDMGCNPEV TGWSRANTND IDLVLEMDGI RETGILMSIS DPHILIKMGL PGREAAREMY
LDALQYAVDH GLRTRAHLED ITRADLEGFV YPLVREIIDI DRDCTIRICD TLGYGLPFEG
MNDPYSIPNM VRRLREIGVK NIETHIHDDF GFGTVNSIVG YWYGANWSNL TFLGIGERAG
NAELEKVLLF LKTRVEGFEK YDLSCLTEFA QFMEEHVGIR VPRNKAVVGR NIFSHESGIH
TAGVIKNPFT YEPYPPEIVG ASRSLMIGPT SGREVLKIKV EEALRDLIDM DVTINKDDWR
LNLIHSEIKR LYDEEKRRSC ISDEELKAYV EKYFLFESIF EDESHTSGEP ISD
//
