ID   CIMA_METMA              Reviewed;         483 AA.
AC   P58966;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=MM_0671;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(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; AE008384; AAM30367.1; -; Genomic_DNA.
DR   AlphaFoldDB; P58966; -.
DR   SMR; P58966; -.
DR   STRING; 192952.MM_0671; -.
DR   EnsemblBacteria; AAM30367; AAM30367; MM_0671.
DR   KEGG; mma:MM_0671; -.
DR   PATRIC; fig|192952.21.peg.797; -.
DR   eggNOG; arCOG02092; Archaea.
DR   HOGENOM; CLU_022158_0_1_2; -.
DR   OMA; SNMFAHE; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000000595; 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_0000140452"
FT   DOMAIN          1..245
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   483 AA;  52040 MW;  F930741357CE86C9 CRC64;
     MRDGEQTPGV ALTKEKKLLI ARALDEMKIN VIEAGSAITS AGERESVRAV ANAGLSAEIC
     SYCRIVKTDV DHALECDVDS IHLVVPVSDL HIRTKIKKDR DTVRQIAADV TEYAKEHGLI
     VELSGEDSSR ADLGFLKAVY SDGIDAGADR LCFCDTVGLL VPEKTTEIFR DLSSSLKAPI
     SIHCHNDFGL ATANTVAALA AGAKQAHVTI NGLGERAGNA SLEEVVMCLE WLYKYDTGIK
     HEQIYRTSRL VSRLTGIPVS PNKALVGGNA FTHEAGIHVH GLLADKATYE PMSPEYIGRQ
     RQIVLGKHAG RSSITLALKE MGLEADDAQT EEIFNRVKQM GDQGKHVTDA DLQIIAETVL
     DIYKEPLVKL EEFTIVSGNR VTPTASIKLN VKDKEIVQAG IGNGPVDAVI NAIRRAVSSC
     AEDVILEEYH VDAVTGGTDA LVEVRVKLSK EGKSITASGA RTDIIMASVE AVMNGLNRLV
     RAE