ID G7WQ96_METH6 Unreviewed; 393 AA.
AC G7WQ96;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:AET65288.1};
GN OrderedLocusNames=Mhar_1932 {ECO:0000313|EMBL:AET65288.1};
OS Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET65288.1, ECO:0000313|Proteomes:UP000005877};
RN [1] {ECO:0000313|EMBL:AET65288.1, ECO:0000313|Proteomes:UP000005877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6Ac {ECO:0000313|EMBL:AET65288.1,
RC ECO:0000313|Proteomes:UP000005877};
RX PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT "The genome characteristics and predicted function of methyl-group
RT oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT spp.";
RL PLoS ONE 7:E36756-E36756(2012).
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, ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP003117; AET65288.1; -; Genomic_DNA.
DR RefSeq; WP_014587466.1; NC_017527.1.
DR AlphaFoldDB; G7WQ96; -.
DR STRING; 1110509.Mhar_1932; -.
DR GeneID; 12511105; -.
DR KEGG; mhi:Mhar_1932; -.
DR PATRIC; fig|1110509.7.peg.2139; -.
DR HOGENOM; CLU_022158_4_2_2; -.
DR OrthoDB; 6555at2157; -.
DR Proteomes; UP000005877; 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 CDD; cd07940; DRE_TIM_IPMS; 1.
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; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005877};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 20..270
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 393 AA; 43936 MW; 67F47FDB15C2292E CRC64;
MQDYSVNQFL ELAKTPKIEI EVCDVTLRDG EQMPGVVFRP DEKIDIAIKL DEVGVEIIEA
GFPVVSEAEM RAVRDVSNLG LDSKISVLSR SVPKDVDAAL ACDVDMVSVF IATSDLHLKY
KLHMTCEEAI KSALETVEYA KDHGLIVRFS AEDATRTEFN LLKRLYKKAE ECRADYVSIA
DTVGIMNPRT VYFLVREIKK VVKIPICMHC HDDLGLALAN TLAAAEAGAK QLHTTVNGIG
ERSGNTPLEE LMVALRVHYS VDRYDTTKLT DLSKLVQSYS GVMMPKNKAV VGDNAFAHES
GIHVAAVLEE PRTYELYSPE MVGSARRIII GKHTGARALK YITKKMGYDL KRDEICLLAE
RVKRCSEFKR PISCDELRKL IHDLDIEIVY PDL
//
