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Database: UniProt
Entry: V7EPK2_9RHOB
LinkDB: V7EPK2_9RHOB
Original site: V7EPK2_9RHOB 
ID   V7EPK2_9RHOB            Unreviewed;       541 AA.
AC   V7EPK2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   ORFNames=Q27BPR15_03170 {ECO:0000313|EMBL:ESW62082.1};
OS   Rhodobacter sp. CACIA14H1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=1408890 {ECO:0000313|EMBL:ESW62082.1, ECO:0000313|Proteomes:UP000018503};
RN   [1] {ECO:0000313|EMBL:ESW62082.1, ECO:0000313|Proteomes:UP000018503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24435858;
RA   Lima A.R., Siqueira A.S., Dos Santos B.G., da Silva F.D., Inada D.T.,
RA   Lima C.P., Cardoso J.F., Vianez-Junior J.L., Nunes M.R., Goncalves E.C.;
RT   "Draft Genome Sequence of Rhodobacter sp. Strain CACIA 14H1, a
RT   Heterotrophic Bacterium Obtained from a Nonaxenic Culture of a Cyanobium
RT   Species.";
RL   Genome Announc. 2:e01116-13(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESW62082.1}.
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DR   EMBL; AYNO01000012; ESW62082.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7EPK2; -.
DR   STRING; 1408890.Q27BPR15_03170; -.
DR   PATRIC; fig|449393.3.peg.648; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000018503; 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:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018503};
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   541 AA;  58266 MW;  43E144DBE951DF36 CRC64;
     MKERLYLFDT TLRDGQQTQG VQFSTPEKRQ IAAALDVLGV DYIEGGWPGA NPTDSEFFAD
     APRTRARMTA FGMTKRVGRS AENDDVLAAV LDAGTAAVCL VGKTHEFHVR TALGCTLEEN
     VEAIRASVAH CVAKEREALF DAEHFFDGYR ADPAYALTCL RAALEAGARW VVLCDTNGGT
     LPAEVGRVVG EVIAAGVPGD RLGIHCHDDT GNAVANSLAA VDAGCRQIQG TLNGLGERCG
     NANLTTIIPT LLLKAPYAER FETGVSREAL AGMVRISRQL DDILNRVPLR SAPYVGASAF
     AHKAGLHASA ILKDPSTYEH VDPSVVGNER VIPMSNQAGQ SNLRARLAAA GIEVDPKDAR
     LGRILEVVKE REDQGYAYDG AQASFELVAR AELGLLPEFF EVKRYRVTVE RRKNKYNRMV
     SLSEAVVVVK IGEAKMLSVS ESMDETGTDR GPVNALAKAL GKDLGPYQAV IDDMKLVDFK
     VRITQGGTEA VTRVIIDSED SQGRRWSTVG VSANIVDASF EALLDAINWK LIRDVGEPVG
     A
//
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