ID A0A1H7E1F7_9RHOB Unreviewed; 545 AA.
AC A0A1H7E1F7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=SAMN05444007_11716 {ECO:0000313|EMBL:SEK06887.1};
OS Cribrihabitans marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cribrihabitans.
OX NCBI_TaxID=1227549 {ECO:0000313|EMBL:SEK06887.1, ECO:0000313|Proteomes:UP000199379};
RN [1] {ECO:0000313|EMBL:SEK06887.1, ECO:0000313|Proteomes:UP000199379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29340 {ECO:0000313|EMBL:SEK06887.1,
RC ECO:0000313|Proteomes:UP000199379};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00034270};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from pyruvate: step 1/3. {ECO:0000256|ARBA:ARBA00004743}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154, ECO:0000256|RuleBase:RU003523}.
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DR EMBL; FNYD01000017; SEK06887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7E1F7; -.
DR STRING; 1227549.SAMN05444007_11716; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000199379; Unassembled WGS sequence.
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 CDD; cd07941; DRE_TIM_LeuA3; 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 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 NCBIfam; TIGR00977; citramal_synth; 1.
DR PANTHER; PTHR43538:SF1; (R)-CITRAMALATE SYNTHASE; 1.
DR PANTHER; PTHR43538; ALPHA-IPM SYNTHASE/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; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Reference proteome {ECO:0000313|Proteomes:UP000199379};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 6..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 545 AA; 58885 MW; 9BA2343D7EE658E0 CRC64;
MSSERLYLYD TTLRDGQQTQ GVQFSTAEKV RIAEALDALG VDYIEGGWPG ANPTDSAFFD
ASPETRARLT AFGMTKRAGR SADNDEVLAA VMNAGTGTVC LVGKTHDYHV HHALGVALEE
NTENVRASIA HVVAQGREAL FDAEHFFDGY RDNPDYALEV CRAALEAGAR WIVLCDTNGG
TLAGEVGRIV GEVIAAGIPG DRLGIHTHND TEQAVAGSLA AVEAGARQIQ GTLNGLGERC
GNANLTSLIP TLLLKERYAE RFETGVSLEA LAGLTRTSRM LDEILNRVPM KQAPYVGASA
FAHKAGLHAS AILKDPATYE HVDPATVGNT RIIPMSNQAG QSNLRNRLAE AGLEVEPGDP
ALGRILERVK ARETEGYSYD TAQASFELLA REELGRLPEF FEVKRYKVTI ERRKNKRNRM
VSLSEAVVVV KVDGEKRLSV SESFDELGED RGPVNALARA LAKDLGQYSG LLADMRLVDF
KVRITQGGTE AVTRVIIDSE DGKGRRWSTV GVSANIVDAS FEALTDAIKW KLIRDCGAPH
GRNGV
//
