ID   CIMA_GEOSL              Reviewed;         528 AA.
AC   Q74C76;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000305};
DE            EC=2.3.1.182 {ECO:0000269|PubMed:18245290};
DE   AltName: Full=Citramalate synthase {ECO:0000303|PubMed:18245290};
GN   Name=cimA {ECO:0000303|PubMed:18245290, ECO:0000312|EMBL:AAR35175.1};
GN   OrderedLocusNames=GSU1798 {ECO:0000312|EMBL:AAR35175.1};
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=18245290; DOI=10.1128/jb.01841-07;
RA   Risso C., Van Dien S.J., Orloff A., Lovley D.R., Coppi M.V.;
RT   "Elucidation of an alternate isoleucine biosynthesis pathway in Geobacter
RT   sulfurreducens.";
RL   J. Bacteriol. 190:2266-2274(2008).
CC   -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC       to form (R)-citramalate. Makes part of the main pathway for isoleucine
CC       biosynthesis in G.sulfurreducens, i.e. the citramalate-dependent
CC       pathway. {ECO:0000269|PubMed:18245290}.
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:18245290};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from pyruvate: step 1/3. {ECO:0000269|PubMed:18245290}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a great reduction in
CC       citramalate synthase activity and are capable of growth in the absence
CC       of isoleucine, whereas mutants lacking both cimA and the threonine
CC       ammonia-lyase tcdB are auxotrophs for isoleucine.
CC       {ECO:0000269|PubMed:18245290}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; AE017180; AAR35175.1; -; Genomic_DNA.
DR   RefSeq; NP_952848.1; NC_002939.5.
DR   RefSeq; WP_010942443.1; NC_002939.5.
DR   AlphaFoldDB; Q74C76; -.
DR   SMR; Q74C76; -.
DR   STRING; 243231.GSU1798; -.
DR   EnsemblBacteria; AAR35175; AAR35175; GSU1798.
DR   KEGG; gsu:GSU1798; -.
DR   PATRIC; fig|243231.5.peg.1836; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_7_0_7; -.
DR   InParanoid; Q74C76; -.
DR   OMA; KSWDFHV; -.
DR   BioCyc; MetaCyc:MON-21277; -.
DR   BRENDA; 2.3.1.182; 7676.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000000577; 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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Isoleucine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..528
FT                   /note="(R)-citramalate synthase"
FT                   /id="PRO_0000430579"
FT   DOMAIN          4..266
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   528 AA;  59071 MW;  14F74796B8EB1F3E CRC64;
     MSLVKLYDTT LRDGTQAEDI SFLVEDKIRI AHKLDEIGIH YIEGGWPGSN PKDVAFFKDI
     KKEKLSQAKI AAFGSTRRAK VTPDKDHNLK TLIQAEPDVC TIFGKTWDFH VHEALRISLE
     ENLELIFDSL EYLKANVPEV FYDAEHFFDG YKANPDYAIK TLKAAQDAKA DCIVLCDTNG
     GTMPFELVEI IREVRKHITA PLGIHTHNDS ECAVANSLHA VSEGIVQVQG TINGFGERCG
     NANLCSIIPA LKLKMKRECI GDDQLRKLRD LSRFVYELAN LSPNKHQAYV GNSAFAHKGG
     VHVSAIQRHP ETYEHLRPEL VGNMTRVLVS DLSGRSNILA KAEEFNIKMD SKDPVTLEIL
     ENIKEMENRG YQFEGAEASF ELLMKRALGT HRKFFSVIGF RVIDEKRHED QKPLSEATIM
     VKVGGKIEHT AAEGNGPVNA LDNALRKALE KFYPRLKEVK LLDYKVRVLP AGQGTASSIR
     VLIESGDKES RWGTVGVSEN IVDASYQALL DSVEYKLHKS EEIEGSKK