ID M1WUQ0_PSEP2 Unreviewed; 531 AA.
AC M1WUQ0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN OrderedLocusNames=BN4_10485 {ECO:0000313|EMBL:CCH47723.1};
OS Pseudodesulfovibrio piezophilus (strain DSM 21447 / JCM 15486 / C1TLV30)
OS (Desulfovibrio piezophilus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae.
OX NCBI_TaxID=1322246 {ECO:0000313|EMBL:CCH47723.1, ECO:0000313|Proteomes:UP000011724};
RN [1] {ECO:0000313|EMBL:CCH47723.1, ECO:0000313|Proteomes:UP000011724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX PubMed=23383081; DOI=10.1371/journal.pone.0055130;
RA Pradel N., Ji B., Gimenez G., Talla E., Lenoble P., Garel M., Tamburini C.,
RA Fourquet P., Lebrun R., Bertin P., Denis Y., Pophillat M., Barbe V.,
RA Ollivier B., Dolla A.;
RT "The first genomic and proteomic characterization of a deep-sea sulfate
RT reducer: insights into the piezophilic lifestyle of Desulfovibrio
RT piezophilus.";
RL PLoS ONE 8:e55130-e55130(2013).
RN [2] {ECO:0000313|Proteomes:UP000011724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
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; FO203427; CCH47723.1; -; Genomic_DNA.
DR RefSeq; WP_015413778.1; NC_020409.1.
DR AlphaFoldDB; M1WUQ0; -.
DR STRING; 1322246.BN4_10485; -.
DR KEGG; dpi:BN4_10485; -.
DR PATRIC; fig|879567.3.peg.506; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_7_0_7; -.
DR OrthoDB; 9803573at2; -.
DR BioCyc; DPIE1322246:BN4_RS02525-MONOMER; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000011724; 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:CCH47723.1};
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:UP000011724};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 4..270
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 531 AA; 58636 MW; B36C165B2955CE18 CRC64;
MKKITIYDTT LRDGAQAEEL NLTTEDKIRI AHKLDELGIH YIEAGWPGSN PTDKKFFDEI
KKHTFEFARL TAFGSTHLAK KTPAQDANLN ALLAAETSVI TIFGKSWDLH ATTALGIPLE
RNLELISNSI DYLCQRVDEV IFDAEHFFDG YKNNPEYALK ALKAAYQAGA SRLILCDTNG
GTLTHEVAAT ISAVRKALPN ASLGIHAHND SEMAVANSIE AVRLGACQVQ GTINGYGERC
GNANLCSVIP NLELKMGLET IGQGNLERLT STSHYISEIA NLRPFMRQPF VGASAFAHKG
GIHVSAILKD AKTYEHIIPE TVGNEQRVLL SDQAGKSNIL FKARELGYEL GKNDPTVDLL
LRELKQKESM GYEYSVADAS FELVLLEALG TPLNYFRFQN FFVVDAKREE DAEPFTEATV
IVDVKGQVEH TAATGMGPVN ALDRALRKGL ERFYPKLSEV KLLDFKVRVL SGAVRDTGGT
ASFVRVLIET GDKHERWTTM GVSHNIIEAS WQAVVDSVNY KLFKDDLRDT L
//
