ID   CIMA_METAC              Reviewed;         483 AA.
AC   Q8TJJ1;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Putative (R)-citramalate synthase CimA {ECO:0000255|HAMAP-Rule:MF_01028};
DE            EC=2.3.1.182 {ECO:0000255|HAMAP-Rule:MF_01028};
GN   Name=cimA {ECO:0000255|HAMAP-Rule:MF_01028}; OrderedLocusNames=MA_3793;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
CC   -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC       to form (R)-citramalate. {ECO:0000255|HAMAP-Rule:MF_01028}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01028};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from pyruvate: step 1/3. {ECO:0000255|HAMAP-
CC       Rule:MF_01028}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01028}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01028}.
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DR   EMBL; AE010299; AAM07144.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TJJ1; -.
DR   SMR; Q8TJJ1; -.
DR   STRING; 188937.MA_3793; -.
DR   EnsemblBacteria; AAM07144; AAM07144; MA_3793.
DR   KEGG; mac:MA_3793; -.
DR   HOGENOM; CLU_022158_0_1_2; -.
DR   InParanoid; Q8TJJ1; -.
DR   OMA; SNMFAHE; -.
DR   PhylomeDB; Q8TJJ1; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000002487; 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; 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..483
FT                   /note="Putative (R)-citramalate synthase CimA"
FT                   /id="PRO_0000140449"
FT   DOMAIN          1..245
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   483 AA;  52274 MW;  1020708EFCAE18F7 CRC64;
     MRDGEQTPGV ALTREKKLLI ARALDEMRIN VIEAGSAITS AGERESIKAV ANAGLDAEIC
     SYCRIVKMDV DHALECDVDS IHLVAPVSDL HIKTKIKKDR DTVRQIAAEV TEYAKDHGLI
     VELSGEDASR ADPEFLKAIY SDGIDAGADR LCFCDTVGLL VPEKTTEIFR DLSSSLKAPI
     SIHCHNDFGL ATANTVAALA AGAKQSHVTI NGLGERAGNA SLEEVVMSLE WLYKYDTGIK
     HEQIYRTSRL VSRLTGIPVS PNKALVGGNA FTHEAGIHVH GLLADKSTYE PMSPEYIGRQ
     RQIVLGKHAG RSSITLALKE MGLEADEAQT EEIFNRVKQM GDQGKHITDA DLQTIAETVL
     DIYKEPIVKL EEFTIVSGNR VTPTASIKLN VKDKEIVQAG IGNGPVDAVI NAIRRAVSSC
     AEDVVLEEYH VDSITGGTDA LVEVRVKLSK NGKVITASGA RTDIIMASVE AVMNGMNRLI
     REE