ID A0A1G5Q6U3_9RHOB Unreviewed; 538 AA.
AC A0A1G5Q6U3;
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=SAMN04488118_103105 {ECO:0000313|EMBL:SCZ57595.1};
OS Epibacterium ulvae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Epibacterium.
OX NCBI_TaxID=1156985 {ECO:0000313|EMBL:SCZ57595.1, ECO:0000313|Proteomes:UP000198767};
RN [1] {ECO:0000313|EMBL:SCZ57595.1, ECO:0000313|Proteomes:UP000198767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U95 {ECO:0000313|EMBL:SCZ57595.1,
RC ECO:0000313|Proteomes:UP000198767};
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; FMWG01000003; SCZ57595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5Q6U3; -.
DR STRING; 1156985.SAMN04488118_103105; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000198767; 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:UP000198767};
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 538 AA; 58172 MW; 321A25DB51D06068 CRC64;
MPTERLYLYD TTLRDGQQTQ GVQFSTEEKK QIATALDHLG VDYIEGGWPG ANPTDSAFFE
EAPATTARMT AFGMTKRAGR SAENDDVLAA VLNAGTAAVC LVGKSHDYHV TQALGINLDE
NIENIKASIM HIKAQGREAL FDAEHFFDGY HDNADYALRC CKAAYDAGAR WVVLCDTNGG
AQPSTISHVV KEVIAAGIPG SHLGIHTHND TEQAVACSLA AVEAGVRQVQ GTLNGLGERC
GNANLVSLIP TLLLKDPYAS LVHTGVSDTA LADLTKVSRM LDDILNRVPS KQSPYVGASA
FAHKAGLHAS AILKDPSTYE HVDPAVVGNA RIIPMSNQAG QSNLRKRLSD AGLVVEKGDP
RLAQILDRIK EREAKGYSYD TAQASFELLA RAELGDMPEF FEVKRYKVTV ERRKNKYNQM
ISLSEAVVVV KVDGEKRLSV SESLDDDGGD RGPVNALAKA LRKDLGRYSA PLDDMHLVDF
KVRITQGGTA AATRVIIDYE DGQGRRWSTV GVSPNIIDAS FEALLDGINW KLLHDGTD
//
