ID   Y1888_STAEQ             Reviewed;         317 AA.
AC   Q5HLU4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase SERP1888;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=SERP1888;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; CP000029; AAW55277.1; -; Genomic_DNA.
DR   RefSeq; WP_001832639.1; NC_002976.3.
DR   AlphaFoldDB; Q5HLU4; -.
DR   SMR; Q5HLU4; -.
DR   STRING; 176279.SERP1888; -.
DR   EnsemblBacteria; AAW55277; AAW55277; SERP1888.
DR   GeneID; 50018020; -.
DR   KEGG; ser:SERP1888; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_2_9; -.
DR   OMA; KMKPNCI; -.
DR   OrthoDB; 1638924at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome.
FT   CHAIN           1..317
FT                   /note="Putative 2-hydroxyacid dehydrogenase SERP1888"
FT                   /id="PRO_0000312189"
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;  34736 MW;  606478610CD419DF CRC64;
     MTKVYIAGAI PEVGLNLLKE HFEVDMYDGE GLIDKETLKK GVEHADALIS LLSTSVDKDI
     IDSANNLKII ANYGAGFNNI DVEYARQQNI DVTNTPHAST NATADLTIGL ILSVARRIVE
     GDHLSRTTGF DGWAPLFFRG REVSGKTIGI IGLGEIGGAV AKRARAFDMD VLYTGPHRKE
     EKERDIGAKY VDLDTLLKNA DFITINAAYN PSLHHMIDTE QFNKMKSTAY LINAGRGPIV
     NEQSLVEALD NKAIEGAALD VYEFEPEITD ALKSFKNVVL TPHIGNATFE ARDMMAKIVA
     NDTIKKLNGD EPQFIVN