ID   CIMA_METTH              Reviewed;         496 AA.
AC   O26819;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Putative (R)-citramalate synthase CimA {ECO:0000255|HAMAP-Rule:MF_01028};
DE            EC=2.3.1.182 {ECO:0000255|HAMAP-Rule:MF_01028};
GN   Name=cimA {ECO:0000255|HAMAP-Rule:MF_01028}; OrderedLocusNames=MTH_723;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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=2.3.1.182; 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; AE000666; AAB85228.1; -; Genomic_DNA.
DR   PIR; F69196; F69196.
DR   RefSeq; WP_010876362.1; NC_000916.1.
DR   AlphaFoldDB; O26819; -.
DR   SMR; O26819; -.
DR   STRING; 187420.MTH_723; -.
DR   EnsemblBacteria; AAB85228; AAB85228; MTH_723.
DR   GeneID; 1470684; -.
DR   KEGG; mth:MTH_723; -.
DR   PATRIC; fig|187420.15.peg.708; -.
DR   HOGENOM; CLU_022158_0_1_2; -.
DR   OMA; SNMFAHE; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:UniProtKB-EC.
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   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.160.270; -; 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   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF08502; LeuA_dimer; 1.
DR   SMART; SM00917; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; SSF110921; 1.
DR   TIGRFAMs; TIGR02090; LEU1_arch; 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; Reference proteome; Transferase.
FT   CHAIN           1..496
FT                   /note="Putative (R)-citramalate synthase CimA"
FT                   /id="PRO_0000140453"
FT   DOMAIN          3..253
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   496 AA;  53705 MW;  FCB4D5CDC2F5A115 CRC64;
     MQVRVLDTTL RDGEQTPGVS LTPEEKLRIA LKIDALGADI IEAGSAITSE GEREGIRKIT
     SEGLRAEICS FARAVREDID AAISCDVDSV HLVVPTSDLH LEHKLRKTRE EVLEQAVDCT
     EYAVDHGILV ELSAEDSTRS DMDFLRTIFR EGIEAGAERI CACDTVGILT PERSYEFYRG
     LSELGAPLSV HCHNDFGLAV ANSLAGLRAG ASEVHATING IGERAGNAAL EEVVVALKSL
     YDVDTSINIE MLYETSRMVA RMTGVYLQPN KAIVGENAFA HESGIHADGV LKKAETYEPI
     TPEMVGHGRG FVMGKHIGTH ALRKRLDELG MKVADDKLME IFRRVKTLGD MGKCVTDVDL
     QAIAEDVLGV MEDKVVDLQE VTIVSGNRVT PTASVKLRVD DREVLEAGTG VGPVDAAIVA
     IKKSLEDFAD ITLEEYHVDA ITGGTDALID VVIKLRHGDR IISARSTQPD IIMASVEAFL
     SGVNRLLANE KSEGTH