ID G7WM10_METH6 Unreviewed; 500 AA.
AC G7WM10;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=cimA {ECO:0000256|HAMAP-Rule:MF_01028};
GN OrderedLocusNames=Mhar_1016 {ECO:0000313|EMBL:AET64385.1};
OS Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET64385.1, ECO:0000313|Proteomes:UP000005877};
RN [1] {ECO:0000313|EMBL:AET64385.1, ECO:0000313|Proteomes:UP000005877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6Ac {ECO:0000313|EMBL:AET64385.1,
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 -!- 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, ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP003117; AET64385.1; -; Genomic_DNA.
DR RefSeq; WP_014586570.1; NC_017527.1.
DR AlphaFoldDB; G7WM10; -.
DR STRING; 1110509.Mhar_1016; -.
DR GeneID; 12510185; -.
DR KEGG; mhi:Mhar_1016; -.
DR PATRIC; fig|1110509.7.peg.1133; -.
DR HOGENOM; CLU_022158_0_1_2; -.
DR OrthoDB; 6555at2157; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000005877; Chromosome.
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; IPR011830; LEU1_arch.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR02090; LEU1_arch; 1.
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; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000005877};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01028}.
FT DOMAIN 10..260
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 500 AA; 53364 MW; 1421C7C84653F657 CRC64;
MRGIALFGRV RLLDTTLRDG EQTPGVSLTL EEKVSIARQL DALGLDVIEA GSAVTSEGER
RAMKAVAEEG LRAEVCSYVR ARTGDVDLAL NCDVDSIHLV VPVSDLHIRC KLRSDREGVM
RAAVEVTEYA KGHGLIVELS GEDASRADEG YLTALYRAGI DAGADRLCYC DTVGVLVAEK
AFEVFSRLSK LPVPVSVHCH DDFGLATANT VAALRGGASM AHVTVNGIGE RGGNTSLEEV
VMTLESLYGI KTEIQCQELY SLSRLVSRLT GIPVAPNKAI VGENAFTHEA GIHVHGLLAD
TSTYEPIHPE AVGRKRRIVL GKHAGRSSVE LALRELGIES TEGELAEILS RVKELGDKGK
RVTDADLQTI AEIVLSIQKE PKVKLNEFTI VSGNHAIPTA SVRIIVNGSE ILEAGTGVGP
VDAAINAIRR AISGVRDVRL EEYHVDAVTG GTNALVEVWV TMAMGDRTIT ARGAGADIIM
ASVEAVLEGI NRLMQLEEDG
//
