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Database: UniProt
Entry: Q8TYM1
LinkDB: Q8TYM1
Original site: Q8TYM1 
ID   CIMA_METKA              Reviewed;         509 AA.
AC   Q8TYM1;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-NOV-2023, entry version 99.
DE   RecName: Full=Putative (R)-citramalate synthase CimA;
DE            EC=2.3.3.21;
GN   Name=cimA; OrderedLocusNames=MK0275;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC   Methanopyraceae; Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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=2.3.3.21;
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; AE009439; AAM01492.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TYM1; -.
DR   SMR; Q8TYM1; -.
DR   STRING; 190192.MK0275; -.
DR   PaxDb; 190192-MK0275; -.
DR   EnsemblBacteria; AAM01492; AAM01492; MK0275.
DR   KEGG; mka:MK0275; -.
DR   PATRIC; fig|190192.8.peg.278; -.
DR   HOGENOM; CLU_022158_0_1_2; -.
DR   InParanoid; Q8TYM1; -.
DR   OMA; SNMFAHE; -.
DR   OrthoDB; 6555at2157; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:InterPro.
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   CDD; cd07940; DRE_TIM_IPMS; 1.
DR   Gene3D; 1.10.238.260; -; 1.
DR   Gene3D; 3.30.160.270; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR02090; LEU1_arch; 1.
DR   PANTHER; PTHR42880:SF2; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR   PANTHER; PTHR42880; HOMOCITRATE SYNTHASE; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF08502; LeuA_dimer; 1.
DR   SMART; SM00917; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR   SUPFAM; SSF51569; Aldolase; 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..509
FT                   /note="Putative (R)-citramalate synthase CimA"
FT                   /id="PRO_0000140413"
FT   DOMAIN          14..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   509 AA;  55687 MW;  0FC96764B11D80BF CRC64;
     MREANADADP PDEVRIFDTT LRDGEQTPGV ALTPEEKLRI ARKLDEIGVD TIEAGFAAAS
     EGELKAIRRI AREELDAEVC SMARMVKGDV DAAVEAEADA VHIVVPTSEV HVKKKLRMDR
     EEVLERAREV VEYARDHGLT VEISTEDGTR TELEYLYEVF DACLEAGAER LGYNDTVGVM
     APEGMFLAVK KLRERVGEDV ILSVHCHDDF GMATANTVAA VRAGARQVHV TVNGIGERAG
     NAALEEVVVV LEELYGVDTG IRTERLTELS KLVERLTGVR VPPNKAVVGE NAFTHESGIH
     ADGILKDEST YEPIPPEKVG HERRFVLGKH VGTSVIRKKL KQMGVDVDDE QLLEILRRLK
     RLGDRGKRIT EADLRAIAED VLGRPAERDI EVEDFTTVTG KRTIPTASIV VKIDGTRKEA
     ASTGVGPVDA TIKALERALK DQGIDFELVE YRAEALTGGT DAITHVDVKL RDPETGDIVH
     SGSSREDIVV ASLEAFIDGI NSLMARKRS
//
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