ID A0A0C4YGF8_9BURK Unreviewed; 293 AA.
AC A0A0C4YGF8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=D-lactate dehydratase {ECO:0000256|ARBA:ARBA00013134};
DE EC=4.2.1.130 {ECO:0000256|ARBA:ARBA00013134};
GN ORFNames=RR42_s3366 {ECO:0000313|EMBL:AJG24942.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG24942.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG24942.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG24942.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methylglyoxal = (R)-lactate + H(+);
CC Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130;
CC Evidence={ECO:0000256|ARBA:ARBA00001524};
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DR EMBL; CP010537; AJG24942.1; -; Genomic_DNA.
DR RefSeq; WP_043357317.1; NZ_CP010537.1.
DR AlphaFoldDB; A0A0C4YGF8; -.
DR STRING; 68895.RR42_s3366; -.
DR KEGG; cbw:RR42_s3366; -.
DR OrthoDB; 9792284at2; -.
DR Proteomes; UP000031843; Chromosome secondary.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0036524; F:protein deglycase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR InterPro; IPR017283; HchA.
DR PANTHER; PTHR48094:SF11; GLUTATHIONE-INDEPENDENT GLYOXALASE HSP31-RELATED; 1.
DR PANTHER; PTHR48094; PROTEIN/NUCLEIC ACID DEGLYCASE DJ-1-RELATED; 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR PIRSF; PIRSF037798; Chaperone_HchA; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Reference proteome {ECO:0000313|Proteomes:UP000031843};
KW Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT DOMAIN 77..198
FT /note="DJ-1/PfpI"
FT /evidence="ECO:0000259|Pfam:PF01965"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 293 AA; 32120 MW; 94BC3FE2FBB81A5B CRC64;
MTSQTDSKQP TPDPAERNAF FPSPYSLSQF TSPKSNLADA DYPDAYQGGR WKVLLVAADE
RYLLTGNGTF FSTGNHPVET LLPMYHLDRA GFEFDIATLS GNPAKFEWWA FPSEDAEIKA
LYAKYEQKFQ QPLKLADVVN SLNKDADYIA VFVPGGHGAL MGLPFSADMK ATLQWAMQND
KYVITLCHGP AALLSASVDE PNGGDLFRGY RICAFPDAMD KQTPDIGYMP GPLRWFFGEK
LAAMGVEIVN TGIDGSTFRD RKLLTGDSPL AANNLGKLAA RVLLDEVQNT GGR
//
