ID   CIMA_THEMA              Reviewed;         538 AA.
AC   Q9WZ22;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000305};
DE            EC=2.3.1.182 {ECO:0000250|UniProtKB:Q74C76};
GN   Name=cimA {ECO:0000305}; OrderedLocusNames=TM_0552;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC       to form (R)-citramalate. {ECO:0000250|UniProtKB:Q74C76}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q74C76};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from pyruvate: step 1/3. {ECO:0000250|UniProtKB:Q74C76}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD35637.1; -; Genomic_DNA.
DR   PIR; F72362; F72362.
DR   RefSeq; NP_228362.1; NC_000853.1.
DR   RefSeq; WP_004081335.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WZ22; -.
DR   SMR; Q9WZ22; -.
DR   STRING; 243274.THEMA_01915; -.
DR   EnsemblBacteria; AAD35637; AAD35637; TM_0552.
DR   KEGG; tma:TM0552; -.
DR   eggNOG; COG0119; Bacteria.
DR   InParanoid; Q9WZ22; -.
DR   OMA; KSWDFHV; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000008183; 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-UniPathway.
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   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005675; Citramal_synthase.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR43538; PTHR43538; 1.
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; TIGR00977; citramal_synth; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 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..538
FT                   /note="(R)-citramalate synthase"
FT                   /id="PRO_0000140472"
FT   DOMAIN          3..268
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   538 AA;  60290 MW;  94F3AF0852C59BA1 CRC64;
     MSIKVYDTTL RDGAQAFGVS FSLEDKIRIA EALDDLGVHY LEGGWPGSNP KDIAFFEAVK
     GMNFKNLKVA AFSSTRRPDV KIEEDANIQT LIKAETPVYT IFGKSWDLHV EKALRTTLEE
     NLKMIYDTVS YLKRFADEVI YDAEHFFDGY KANREYALKT LKVAEEAGAD CLVLADTNGG
     TLPHEIEEII EDVKKHVKAP LGIHAHNDSD VAVANTLAAV RKGAVHVQGT INGLGERCGN
     ANLCSVIPNL VLKMGLEVIP KENLKKLFDV AHLVAELSGR PHIENMPYVG DYAFAHKGGV
     HVSAIKRDPR TYEHIDPELV GNRRIISISE LSGKSNVLEK IKEMGFEIDE SSPKVREILK
     KIKELEAQGY HFEGAEASFE LLVRDMLGKR KKYFEFLGFT VMTIKNRDEE SFSEATVKVR
     VPDEVAKRLG HDEPFEHTAA EGEGPVEALD RAVRKALEKF YPSLKDTKLT DYKVRILNEQ
     AGTKATTRVL IESSDGKRRW GTVGVSPNII EASWTALLES LEYKLHKDEE EMRNDEEN