ID   Y752_STAHJ              Reviewed;         318 AA.
AC   Q4L8G4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase SH0752;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=SH0752;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AP006716; BAE04061.1; -; Genomic_DNA.
DR   RefSeq; WP_011275076.1; NC_007168.1.
DR   AlphaFoldDB; Q4L8G4; -.
DR   SMR; Q4L8G4; -.
DR   STRING; 279808.SH0752; -.
DR   PRIDE; Q4L8G4; -.
DR   EnsemblBacteria; BAE04061; BAE04061; SH0752.
DR   KEGG; sha:SH0752; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_2_9; -.
DR   OMA; KMKPNCI; -.
DR   OrthoDB; 1638924at2; -.
DR   Proteomes; UP000000543; 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..318
FT                   /note="Putative 2-hydroxyacid dehydrogenase SH0752"
FT                   /id="PRO_0000312191"
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   318 AA;  34858 MW;  64713A9D033A395F CRC64;
     MEKVYIAGAI PEVGLNLLKE HFEVEMYEGE GIIDKATLME GVKDASALIS ILSTNVDQEV
     IDSASNLKII ANYGAGFNNV DVKYAREKDI DVTNTPKAST ASTAELTFGL VLAVARRIVE
     GDKLSRTQGF DGWAPLFFRG REVSGKTIGI IGLGEIGSAV AKRAKAFDMD ILYTGPHQKK
     EKEREIGAKY VDLNTLLENA DFITINAAYN PDLHHMIDTE QFKLMKSTAY LINAGRGPIV
     NEEALVKALE DKQIEGAALD VYEFEPEITE GLKSLDNVVI TPHIGNATYE ARDMMSKIVA
     NDTIKKLNGE TPQFIVNK