ID W9DTU6_METTI Unreviewed; 390 AA.
AC W9DTU6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Isopropylmalate/homocitrate/citramalate synthase {ECO:0000313|EMBL:ETA66861.1};
DE EC=2.3.3.13 {ECO:0000313|EMBL:ETA66861.1};
GN ORFNames=MettiDRAFT_0264 {ECO:0000313|EMBL:ETA66861.1};
OS Methanolobus tindarius DSM 2278.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=1090322 {ECO:0000313|EMBL:ETA66861.1, ECO:0000313|Proteomes:UP000019483};
RN [1] {ECO:0000313|EMBL:ETA66861.1, ECO:0000313|Proteomes:UP000019483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2278 {ECO:0000313|EMBL:ETA66861.1,
RC ECO:0000313|Proteomes:UP000019483};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (AUG-2013) 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, ECO:0000256|RuleBase:RU003523}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETA66861.1}.
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DR EMBL; AZAJ01000001; ETA66861.1; -; Genomic_DNA.
DR RefSeq; WP_023843997.1; NZ_AZAJ01000001.1.
DR AlphaFoldDB; W9DTU6; -.
DR STRING; 1090322.MettiDRAFT_0264; -.
DR OrthoDB; 6555at2157; -.
DR Proteomes; UP000019483; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004410; F:homocitrate synthase activity; IEA:RHEA.
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 Acyltransferase {ECO:0000313|EMBL:ETA66861.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 23..273
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 390 AA; 42887 MW; FA6B84F932815C6A CRC64;
MSENKDYSRN KLMDYLNLPP LDIEICDVTL RDGEQTPGVV FTREEKIALA TKLDSVGVDI
IEAGFPVVSA GEKEIVKEIA NMGLNSRTCC LSRSRVSDVE VAVDCDVDFI SIFIAMSDLH
LKHKYHKSCE EMFSAAMEAV QYAKDHGVGV RFAAEDGTRT DIEVLKKAFK AAEEYKVDYV
SIADTIGILN PSSTYYLVSE IKKAVNTPIC IHCHNDLGMA TANTLAAAEA GAKQLHTTVN
SIGERAGNAS LEEVLVALRV QYGIDRYDTT KLTELSEMVN QYSGLKPSVT KAIVGEHAFS
HESGIHVCAI LEEPRTYELF SPEMVGGKRH LIVGKHTGMK ALKGIVEEMG HTLSNEELTA
LLDRIKNCTE TKHGISPSRL ETMINETKNQ
//
