GenomeNet

Database: UniProt
Entry: W8RVU9_9RHOB
LinkDB: W8RVU9_9RHOB
Original site: W8RVU9_9RHOB 
ID   W8RVU9_9RHOB            Unreviewed;       539 AA.
AC   W8RVU9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   ORFNames=roselon_03066 {ECO:0000313|EMBL:AHM05339.1};
OS   Roseibacterium elongatum DSM 19469.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseibacterium.
OX   NCBI_TaxID=1294273 {ECO:0000313|EMBL:AHM05339.1, ECO:0000313|Proteomes:UP000019593};
RN   [1] {ECO:0000313|EMBL:AHM05339.1, ECO:0000313|Proteomes:UP000019593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19469 {ECO:0000313|Proteomes:UP000019593};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (MAR-2013) 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}.
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; CP004372; AHM05339.1; -; Genomic_DNA.
DR   RefSeq; WP_025313011.1; NZ_CP004372.1.
DR   AlphaFoldDB; W8RVU9; -.
DR   STRING; 1294273.roselon_03066; -.
DR   KEGG; red:roselon_03066; -.
DR   PATRIC; fig|1294273.3.peg.3027; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_7_0_5; -.
DR   OrthoDB; 9803573at2; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000019593; Chromosome.
DR   GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:RHEA.
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   Acyltransferase {ECO:0000313|EMBL:AHM05339.1};
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:UP000019593};
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   539 AA;  58300 MW;  5C46F27376E265DD CRC64;
     MTERLYLYDT TLRDGQQTQG VQFSTPEKQR IAQALDDLGL DYIEGGWPGA NPTDSAFFEA
     APETRATLTA FGMTKRAGRS AENDDVLAAV MNAGTRSVCL VGKTHDFHVT EALGITLDEN
     VETIRASLAH LVAQGREALF DAEHFFDGYK ANPAYALDCC RAALDAGARW IVLCDTNGGT
     LPGEIGRIVA EVIAAGIPGD RLGIHTHNDT ETAVAGSLAA VEAGARQIQG TLNGLGERCG
     NANLTTLVPT LLLKEPWASR YETGITRDAL KRLTRISRML DDILNRVPTR AAPYVGSSAF
     AHKAGLHASA IVKNPATYEH IDPAEVGNAR IIPMSNQAGQ SNLRRRLSEA GIEVDRANPA
     LAEILTEIKA REDQGYSYDT AQASFELLAR RALGQMPRFF EVKRYRVTVE RRKNKYNETV
     SLSEAVVVVK IGGDKKLSVS ESMDQTGSDR GPVNALAKAL GKDLGPYQSY IDDIRLVDFK
     VRITQGGTEA VTRVVIDSED ATGRRWSTVG VSANIVDASF EALLDAIEWK LVRDGAPAI
//
DBGET integrated database retrieval system