ID   CIMA_ARCFU              Reviewed;         489 AA.
AC   O29305;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Putative (R)-citramalate synthase CimA;
DE            EC=2.3.1.182;
GN   Name=cimA; OrderedLocusNames=AF_0957;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC       to form (R)-citramalate. {ECO:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from pyruvate: step 1/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; AE000782; AAB90286.1; -; Genomic_DNA.
DR   PIR; E69369; E69369.
DR   RefSeq; WP_010878457.1; NC_000917.1.
DR   AlphaFoldDB; O29305; -.
DR   SMR; O29305; -.
DR   STRING; 224325.AF_0957; -.
DR   EnsemblBacteria; AAB90286; AAB90286; AF_0957.
DR   GeneID; 24794558; -.
DR   KEGG; afu:AF_0957; -.
DR   eggNOG; arCOG02092; Archaea.
DR   HOGENOM; CLU_022158_0_1_2; -.
DR   OMA; SNMFAHE; -.
DR   OrthoDB; 10632at2157; -.
DR   PhylomeDB; O29305; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000002199; 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..489
FT                   /note="Putative (R)-citramalate synthase CimA"
FT                   /id="PRO_0000140406"
FT   DOMAIN          3..255
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   489 AA;  53346 MW;  9E84B204DE796F84 CRC64;
     MQVKILDTTL RDGEQTPGVS LSVEQKVMIA EALDNLGVDI IEAGTAIASE GDFQAIKEIS
     QRGLNAEICS FARIKREDID AAADAGAESI FMVAPSSDIH INAKFPGKDR DYVIEKSVEA
     IEYAKERGLI VEFGAEDASR ADLDFVIQLF KRAEEAKADR ITFADTVGVL SPEKMEEIVR
     KIKAKVKLPL AIHCHDDFGL ATANTIFGIK AGAEEFHGTI NGLGERAGNA AIEEVVIALE
     YLYGIKTKIK KERLYNTSKL VEKLSRVVVP PNKPIVGDNA FTHESGIHTS ALFRDAKSYE
     PISPEVVGRK RVIVLGKHAG RASVEAIMNE LGYKATPEQM KEILARIKEI GDKGKRVTDA
     DVRTIIETVL QIKREKKVKL EDLAIFSGKN VMPMASVKLK IDGQERIEAA VGLGPVDAAI
     NAIRRAIKEF ADIKLVSYHV DAITGGTDAL VDVVVQLKKD NKIVTARGAR TDIIMASVEA
     FIEGINMLF