ID A0A0N8KQM2_9EURY Unreviewed; 466 AA.
AC A0A0N8KQM2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Putative (R)-citramalate synthase CimA {ECO:0000256|HAMAP-Rule:MF_01028};
DE EC=2.3.3.21 {ECO:0000256|HAMAP-Rule:MF_01028};
GN Name=leuA {ECO:0000313|EMBL:KPQ42530.1};
GN Synonyms=cimA {ECO:0000256|HAMAP-Rule:MF_01028};
GN ORFNames=MPEBLZ_02912 {ECO:0000313|EMBL:KPQ42530.1};
OS Candidatus Methanoperedens sp. BLZ1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1719120 {ECO:0000313|EMBL:KPQ42530.1, ECO:0000313|Proteomes:UP000050360};
RN [1] {ECO:0000313|EMBL:KPQ42530.1, ECO:0000313|Proteomes:UP000050360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Arshad A., Speth D.R., De Graaf R.M., Op Den Camp H.J., Jetten M.S.,
RA Welte C.U.;
RT "A metagenomics-based metabolic model of nitrate-dependent anaerobic
RT oxidation of methane by Methanoperedens-like archaea.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC to form (R)-citramalate. {ECO:0000256|HAMAP-Rule:MF_01028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+);
CC Xref=Rhea:RHEA:19045, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30934, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.21; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01028};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from pyruvate: step 1/3. {ECO:0000256|HAMAP-
CC Rule:MF_01028}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01028}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154, ECO:0000256|HAMAP-
CC Rule:MF_01028}.
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:KPQ42530.1}.
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DR EMBL; LKCM01000224; KPQ42530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8KQM2; -.
DR PATRIC; fig|1719120.3.peg.3167; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000050360; Unassembled WGS sequence.
DR GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:InterPro.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01028; CimA; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR024890; Citramalate_synthase_CimA.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42880:SF2; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR PANTHER; PTHR42880; HOMOCITRATE SYNTHASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 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 Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01028};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01028};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624, ECO:0000256|HAMAP-
KW Rule:MF_01028};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01028}.
FT DOMAIN 1..226
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 466 AA; 49867 MW; 416E0354643EF2AA CRC64;
MIARKIDSLG VDILEAGSAI TSEGERASIK EIAAAGLNAE ICSYCRIKKE DIDAALGCDV
DSIHLVVPVS DLHIQQKLKK DRDSVRELAA QMTEYAKSHG LIVELSGEDA SRADIEYLKS
VYNAGIDAGA DRLCFCDTVG ILLPENTYEI FTDLSKLRAP VSIHCHNDFG MATANTVCAL
RAGANEAHVT INGIGERAGN TSLEEVVMVL YSLYKYKTSI DIKGLYTTSR LVSRLSGIPV
APNKSIVGGN AFTHEAGIHV HGLLANTATY EPITPELVGR ERKIVLGKHA GRSSVVLALK
ELGLDASEKQ IDDIVIRMKE LGDKGKRVTD ADLQTIAETV LGIYQEAKIK LEELTVVAGN
TVMPTASVRL KVNGNHVVEA GVGTGPVDAA INALKKALSG VADIHLDEYH VDAITGGTDA
LVEVWIKLSK GGKTITARGA RTDIIMASVE AVLEGINRLI QQENNR
//
