ID CIMA_METMJ Reviewed; 503 AA.
AC A3CUF2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Putative (R)-citramalate synthase CimA {ECO:0000255|HAMAP-Rule:MF_01028};
DE EC=2.3.3.21 {ECO:0000255|HAMAP-Rule:MF_01028};
GN Name=cimA {ECO:0000255|HAMAP-Rule:MF_01028}; OrderedLocusNames=Memar_1069;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
CC -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC to form (R)-citramalate. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01028};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from pyruvate: step 1/3. {ECO:0000255|HAMAP-
CC Rule:MF_01028}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01028}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000255|HAMAP-Rule:MF_01028}.
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DR EMBL; CP000562; ABN57002.1; -; Genomic_DNA.
DR RefSeq; WP_011843913.1; NC_009051.1.
DR AlphaFoldDB; A3CUF2; -.
DR SMR; A3CUF2; -.
DR STRING; 368407.Memar_1069; -.
DR GeneID; 76731640; -.
DR KEGG; mem:Memar_1069; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_0_1_2; -.
DR OrthoDB; 6555at2157; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000002146; 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; Branched-chain amino acid biosynthesis;
KW Isoleucine biosynthesis; Transferase.
FT CHAIN 1..503
FT /note="Putative (R)-citramalate synthase CimA"
FT /id="PRO_0000407913"
FT DOMAIN 9..257
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 503 AA; 53275 MW; EA9E955BCE0B7118 CRC64;
MIVLFVEPIR FFDTTLRDGE QTPGVSLTPA GKLEIATHLA DVGVHVIEAG SAAASVGERE
SIRAIADAGL AAECCTYVRA LPGDIDLAAD AGADSVHLVV PVSDLHIAKK LRKTREQVSE
MAWSAVEYAK ERGLVVELSG EDASRADQDF LAEVFREGVE RGADRLCFCD TVGLLTPERA
AAIIPPLLFA PLSIHCHDDL GFGLATTVAA LRAGATCAHV TVNGLGERAG NTSLEELVMA
LEVLYGVDTG IATEELYPLS THVARLTGVP LATNKPIVGE MAFTHESGIH AHGVMRDAST
YEPLQPERVG RRRRIVLGKH SGSAAVEAAL HDMGYAPSAA QLKEIVDRIK RLGDAGMRIT
DADIMAIADT VMEIEFTPCI ELRQFTIVSG SNAIPTASVT MLVRGEEITG AAVGTGPVDA
AIRALQRSVA DVGSVRLDEY SVDAITGGTD ALVDVSVKLS KDGKTVTSRG ARTDIIMASV
EAVIAGMNRL LREEHEDRSQ DSD
//
