ID A0A1X7Q0A1_9RHOB Unreviewed; 547 AA.
AC A0A1X7Q0A1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=SAMN05661107_3403 {ECO:0000313|EMBL:SMH57354.1};
OS Maritimibacter sp. HL-12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=1162418 {ECO:0000313|EMBL:SMH57354.1, ECO:0000313|Proteomes:UP000193836};
RN [1] {ECO:0000313|EMBL:SMH57354.1, ECO:0000313|Proteomes:UP000193836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-12 {ECO:0000313|EMBL:SMH57354.1,
RC ECO:0000313|Proteomes:UP000193836};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FXBQ01000001; SMH57354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7Q0A1; -.
DR STRING; 1162418.SAMN05661107_3403; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000193836; 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; PS00816; AIPM_HOMOCIT_SYNTH_2; 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:UP000193836};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 5..271
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 547 AA; 59038 MW; 4C0CE093E9D14552 CRC64;
MTDRLTLYDT TLRDGQQTQG VQFSVAEKVA IAEALDDLGV DYIEGGWPGA NPTDSDFFEQ
RPQTKATFTA FGMTKRAGRS AANDDVLAQV MNANTPAVCL VGKTHDFHVS TALGITLEEN
LENIRASVAH MVASGREALF DAEHFFDGYK ANAPYALECA LAAYHAGARW VVLCDTNGGT
LPGEIHDITR AVIEAGIPGD NIGIHCHDDT GNAVAGSLAA IDAGARQVQG TLNGLGERCG
NANLVSLIPT LLLKEPYRSA YETGITEAAL TSLTRLSRQL DDILNRVPLR SAPYVGASAF
THKAGLHASA ILKDPTTYEH IPPGLVGNAR LVPMSNQAGQ SNLRRRLAEA GIEIDKGDAR
LGEILDEIKR REDEGYAYDG AQASFEVLAR RMLGQMPRFF EVKRYKVTVE RRKNRYDRMV
SLSEAVVVVK IGDEKKLSVS ESMDETGADR GPVNALAKAL GKDLGPYQAC IDDLKLVDFK
VRITQGGTEA VTRVIIDSED GQGRRWSTVG VSPNIVDASF EALLDAINWK LLRDGVAPVR
DMGVAAQ
//
