ID   Y1879_STAES             Reviewed;         317 AA.
AC   Q8CNB8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase SE_1879;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=SE_1879;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AE015929; AAO05520.1; -; Genomic_DNA.
DR   RefSeq; NP_765434.1; NC_004461.1.
DR   RefSeq; WP_002477137.1; NZ_WBME01000032.1.
DR   AlphaFoldDB; Q8CNB8; -.
DR   SMR; Q8CNB8; -.
DR   STRING; 176280.SE_1879; -.
DR   EnsemblBacteria; AAO05520; AAO05520; SE_1879.
DR   KEGG; sep:SE_1879; -.
DR   PATRIC; fig|176280.10.peg.1836; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_2_9; -.
DR   OMA; KMKPNCI; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..317
FT                   /note="Putative 2-hydroxyacid dehydrogenase SE_1879"
FT                   /id="PRO_0000312190"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        283
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         234..236
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         283..286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   317 AA;  34750 MW;  77F6577E0596F6DF CRC64;
     MTKVYIAGAI PEVGLNLLKE HFEVDMYDGE GLIDKETLKK GVEHADALVS LLSTSVDKDI
     IDSANNLKII ANYGAGFNNI DVEYARQQNI DVTNTPHAST NATADLTIGL ILSVARRIVE
     GDHLSRTTGF DGWAPLFFRG REVSGKTIGI IGLGEIGGAV AKRARAFDMD VLYTGPHRKE
     EKERDIGAKY VDLDTLLKNA DFITINAAYN PSLHHMIDTE QFNKMKSTAY LINAGRGPIV
     NEQSLVEALD NKVIEGAALD VYEFEPEITD ALKSFKNVVL TPHIGNATFE ARDMMAKIVA
     NDTIKKLNGD EPQFIVN