CIMA_METKA
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 03-AUG-2022, entry version 93.
DE RecName: Full=Putative (R)-citramalate synthase CimA;
DE EC=2.3.1.182;
GN Name=cimA; OrderedLocusNames=MK0275;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC 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=2.3.1.182;
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 EnsemblBacteria; AAM01492; AAM01492; MK0275.
DR KEGG; mka:MK0275; -.
DR PATRIC; fig|190192.8.peg.278; -.
DR HOGENOM; CLU_022158_0_1_2; -.
DR OMA; SNMFAHE; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000001826; 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; 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