ID A0A1H2SXQ6_9RHOB Unreviewed; 538 AA.
AC A0A1H2SXQ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=SAMN04488001_0983 {ECO:0000313|EMBL:SDW36297.1};
OS Litoreibacter albidus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=670155 {ECO:0000313|EMBL:SDW36297.1, ECO:0000313|Proteomes:UP000199441};
RN [1] {ECO:0000313|Proteomes:UP000199441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26922 {ECO:0000313|Proteomes:UP000199441};
RA Varghese N., Submissions S.;
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; FNOI01000001; SDW36297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2SXQ6; -.
DR STRING; 670155.SAMN04488001_0983; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000199441; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 6..271
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 538 AA; 58545 MW; 4797C4D348774B76 CRC64;
MTRERLTLFD TTLRDGQQTQ GVQFSTPEKV EIAQMLDGIG IDYIEGGWPG ANPTDSEFFS
NVPRTSATMT AFGMTKRAGR SAENDDVLAA VLNANTPAVC LVGKTHDFHV ETALGISLEE
NLENIEKSFQ HIAAQNRETL FDAEHFFDGY KSNPDYALSC IHAAYGAGAL IVLCDTNGGT
LPAEISEIVG KVIDSGIPGA RLGIHTHNDT ENAVAGSLAA VDAGVRHIQG TLNGLGERCG
NANLTSIIPT LLLKEPYKSR YAIGVKQENL TRLTYASRKL DDILNRVPNK HAAYVGVSAF
AHKAGLHASA ILKDPTTYEH IDPAIVGNTR IIPMSNQAGQ SNLRKRLAEM GLKDIDSNAL
PRILDVIKQR EDDGYSYDTA QASFELLARR ELGLLPKYFE VKRYKVTVER RKNKYDKMIS
LSEAVVVVKV GEDKMLSVSE SLDETGSDRG PVNALSKALA KDLGPYSALI EDMRLVDFKV
RITQGGTEAV TRVIIDSADK QGRRWSTVGV SPNIVDASFE ALLDAINWKL VQEGANVT
//
