ID   CIMA_STRCO              Reviewed;         534 AA.
AC   O86511;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000305};
DE            EC=2.3.1.182 {ECO:0000250|UniProtKB:Q74C76};
GN   Name=cimA {ECO:0000305}; OrderedLocusNames=SCO5529; ORFNames=SC1C2.10;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939124; CAA19977.1; -; Genomic_DNA.
DR   PIR; T29059; T29059.
DR   RefSeq; NP_629663.1; NC_003888.3.
DR   RefSeq; WP_011030295.1; NZ_VNID01000011.1.
DR   AlphaFoldDB; O86511; -.
DR   SMR; O86511; -.
DR   STRING; 100226.SCO5529; -.
DR   GeneID; 1100969; -.
DR   KEGG; sco:SCO5529; -.
DR   PATRIC; fig|100226.15.peg.5616; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_7_0_11; -.
DR   InParanoid; O86511; -.
DR   OMA; NTMRMLV; -.
DR   PhylomeDB; O86511; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000001973; 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..534
FT                   /note="(R)-citramalate synthase"
FT                   /id="PRO_0000140470"
FT   DOMAIN          11..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   534 AA;  57527 MW;  3118EDDD6F732A50 CRC64;
     MTATSELDDS FHVFDTTLRD GAQREGINLT VADKLAIARH LDDFGVGFIE GGWPGANPRD
     TEFFARARQE IDFKHAQLVA FGSTRRAGAN AAEDHQVKAL LDSGAQVITL VAKSHDRHVE
     LALRTTLDEN LAMVADTVSH LKAQGRRVFV DCEHFFDGYR ANPEYAKSVV RTASEAGADV
     VVLCDTNGGM LPAQIQAVVA TVLADTGARL GIHAQDDTGC AVANTLAAVD AGATHVQCTA
     NGYGERVGNA NLFPVVAALE LKYGKQVLPE GRLREMTRIS HAIAEVVNLT PSTHQPYVGV
     SAFAHKAGLH ASAIKVDPDL YQHIDPELVG NTMRMLVSDM AGRASIELKG KELGIDLGGD
     RELVGRVVER VKERELAGYT YEAADASFEL LLRAEAEGRP LKYFEVESWR AITEDRPDGS
     HANEATVKLW AKGERIVATA EGNGPVNALD RSLRVALEKI YPELAKLDLV DYKVRILEGV
     HGTQSTTRVL ISTSDGTGEW ATVGVAENVI AASWQALEDA YTYGLLRAGV APAE