CIMA_AQUAE
ID CIMA_AQUAE Reviewed; 528 AA.
AC O66682;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=(R)-citramalate synthase {ECO:0000305};
DE EC=2.3.1.182 {ECO:0000250|UniProtKB:Q74C76};
GN Name=cimA {ECO:0000305}; OrderedLocusNames=aq_356;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC to form (R)-citramalate. {ECO:0000250|UniProtKB:Q74C76}.
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:0000250|UniProtKB:Q74C76};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from pyruvate: step 1/3. {ECO:0000250|UniProtKB:Q74C76}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000305}.
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DR EMBL; AE000657; AAC06637.1; -; Genomic_DNA.
DR PIR; F70331; F70331.
DR RefSeq; NP_213242.1; NC_000918.1.
DR RefSeq; WP_010880180.1; NC_000918.1.
DR AlphaFoldDB; O66682; -.
DR SMR; O66682; -.
DR STRING; 224324.aq_356; -.
DR EnsemblBacteria; AAC06637; AAC06637; aq_356.
DR KEGG; aae:aq_356; -.
DR PATRIC; fig|224324.8.peg.286; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_7_0_0; -.
DR InParanoid; O66682; -.
DR OMA; KSWDFHV; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000000798; 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 3: Inferred from homology;
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_0000140469"
FT DOMAIN 5..271
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 528 AA; 59215 MW; 1BC6ABAEC35D3F34 CRC64;
MAEKVYIYDT TLRDGSQMEG VSFSLEDKIR IAEKLDDFGI HYIEGGWPYA NPKDNLFFQK
AKKMNFKNAK LTAFGSTRRP NKKVSEDPQV ESLIKAETPV VTIFGKSWDL HVTDALKTTL
EENLNMIYET VEYLKRYVDE VIFDAEHFFD GYKSNPEYAL QVLEAALKGG ADWVVLCDTN
GGTLPHEIYE ITKKVKERFK DANVGIHAHN DSETAVANSL MAVLAGARQV HGTINGIGER
TGNANLCSII PNLQLKLGFD VIPQENLKKL TELANFVAEI INMPLPRNMP YVGESAFAHK
GGVHASAVLK NAKTYEHINP ELVGNKRKIT VSDLAGRSNL VHKLKEFGIE IDPKSPELKK
LIDKIKELEK EGYHFEAAEA SLELLIKRHF GLVKDYFDFD AYRVLIAKRR DDSLPTSEAT
VRLSVEGVEE HTASLGNGPI SALDRALRKA LEEFYPNLKE LQLIDYKVRI INESAGTSAK
VRVLIESTDG KRKWGTVGVS ENVIEASWIA LRDSIVYKLM KDEEEGIL