ID   Q1LS72_CUPMC            Unreviewed;       313 AA.
AC   Q1LS72;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   02-APR-2025, entry version 100.
DE   SubName: Full=2-ketoacid reductase {ECO:0000313|EMBL:ABF07004.1};
DE            EC=1.1.1.79 {ECO:0000313|EMBL:ABF07004.1};
GN   Name=ycdW {ECO:0000313|EMBL:ABF07004.1};
GN   OrderedLocusNames=Rmet_0118 {ECO:0000313|EMBL:ABF07004.1};
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF07004.1, ECO:0000313|Proteomes:UP000002429};
RN   [1] {ECO:0000313|Proteomes:UP000002429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC   {ECO:0000313|Proteomes:UP000002429};
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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DR   EMBL; CP000352; ABF07004.1; -; Genomic_DNA.
DR   RefSeq; WP_011515038.1; NC_007973.1.
DR   AlphaFoldDB; Q1LS72; -.
DR   STRING; 266264.Rmet_0118; -.
DR   KEGG; rme:Rmet_0118; -.
DR   eggNOG; COG0111; Bacteria.
DR   HOGENOM; CLU_019796_1_0_4; -.
DR   Proteomes; UP000002429; Chromosome.
DR   GO; GO:0030267; F:glyoxylate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd12164; GDH_like_2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE NAD-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABF07004.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT   DOMAIN          106..278
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   313 AA;  34369 MW;  AFE266441BD90D72 CRC64;
     MKLQLYVPDG RYAPWIDGFA EVLPEAQCVT WEDSQGQSVD YAVVWRPPVE MLRGRTDLKA
     IFNLGAGVDG ILKLNAQHPD ALPAGVPIIR LDDAGMAAQM AEYVTAAVLR YFRRLDVYDA
     QERAGTWKFQ KPHRRADFTI GVMGVGTLGA HIARTLAGFG FPVRGWSRSP KTVDGVQSFH
     GEDGQAAFLD GLRVLVNVLP LTPETQDIID TGLLHRLAHG AYLINVARGQ HLVEEDLLAA
     VREGQIAGAT LDVFRTEPLP ADHPYWQEPR ITITPHISAL TLREDSIAQI AGKIRLLESG
     KPIAGVVDLQ RGY
//