ID   CIMA_METJA              Reviewed;         491 AA.
AC   Q58787;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=(R)-citramalate synthase CimA;
DE            EC=2.3.1.182;
GN   Name=cimA; OrderedLocusNames=MJ1392;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   SUBUNIT.
RX   PubMed=9864346; DOI=10.1128/jb.181.1.331-333.1999;
RA   Howell D.M., Xu H., White R.H.;
RT   "(R)-citramalate synthase in methanogenic archaea.";
RL   J. Bacteriol. 181:331-333(1999).
CC   -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC       to form (R)-citramalate. {ECO:0000269|PubMed:9864346}.
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:0000269|PubMed:9864346};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from pyruvate: step 1/3. {ECO:0000269|PubMed:9864346}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9864346}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; L77117; AAB99402.1; -; Genomic_DNA.
DR   PIR; G64473; G64473.
DR   RefSeq; WP_010870909.1; NC_000909.1.
DR   AlphaFoldDB; Q58787; -.
DR   SMR; Q58787; -.
DR   STRING; 243232.MJ_1392; -.
DR   EnsemblBacteria; AAB99402; AAB99402; MJ_1392.
DR   GeneID; 1452295; -.
DR   KEGG; mja:MJ_1392; -.
DR   eggNOG; arCOG02092; Archaea.
DR   HOGENOM; CLU_022158_0_1_2; -.
DR   InParanoid; Q58787; -.
DR   OMA; SNMFAHE; -.
DR   OrthoDB; 10632at2157; -.
DR   PhylomeDB; Q58787; -.
DR   BioCyc; MetaCyc:MON-11899; -.
DR   BRENDA; 2.3.1.182; 3260.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000000805; 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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Direct protein sequencing; Isoleucine biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..491
FT                   /note="(R)-citramalate synthase CimA"
FT                   /id="PRO_0000140450"
FT   DOMAIN          3..254
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   CONFLICT        2
FT                   /note="M -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   491 AA;  53493 MW;  9D4FA0EA6F8F3BE5 CRC64;
     MMVRIFDTTL RDGEQTPGVS LTPNDKLEIA KKLDELGVDV IEAGSAITSK GEREGIKLIT
     KEGLNAEICS FVRALPVDID AALECDVDSV HLVVPTSPIH MKYKLRKTED EVLETALKAV
     EYAKEHGLIV ELSAEDATRS DVNFLIKLFN EGEKVGADRV CVCDTVGVLT PQKSQELFKK
     ITENVNLPVS VHCHNDFGMA TANTCSAVLG GAVQCHVTVN GIGERAGNAS LEEVVAALKI
     LYGYDTKIKM EKLYEVSRIV SRLMKLPVPP NKAIVGDNAF AHEAGIHVDG LIKNTETYEP
     IKPEMVGNRR RIILGKHSGR KALKYKLDLM GINVSDEQLN KIYERVKEFG DLGKYISDAD
     LLAIVREVTG KLVEEKIKLD ELTVVSGNKI TPIASVKLHY KGEDITLIET AYGVGPVDAA
     INAVRKAISG VADIKLVEYR VEAIGGGTDA LIEVVVKLRK GTEIVEVRKS DADIIRASVD
     AVMEGINMLL N