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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//