ID   Y2389_STAAR             Reviewed;         317 AA.
AC   Q6GEC9;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase SAR2389;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=SAR2389;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG41370.1; -; Genomic_DNA.
DR   RefSeq; WP_000417008.1; NC_002952.2.
DR   AlphaFoldDB; Q6GEC9; -.
DR   SMR; Q6GEC9; -.
DR   KEGG; sar:SAR2389; -.
DR   HOGENOM; CLU_019796_1_2_9; -.
DR   OMA; KMKPNCI; -.
DR   OrthoDB; 1638924at2; -.
DR   Proteomes; UP000000596; 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; 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.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..317
FT                   /note="Putative 2-hydroxyacid dehydrogenase SAR2389"
FT                   /id="PRO_0000312186"
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;  34675 MW;  4D84B4D3A5D5F19F CRC64;
     MEKVYVAGAI PEVGLKLLQE HFEVEMYEGK GLVDKDTLIK GVKDATALIS LLSTNVDKDV
     IDAGKDLKII ANYGAGFNNI DIEYAREKSI DVTNTPKAST NATADLTIGL VLAVARRIVE
     GDQLSRTTGF DGWAPLFFRG REVSGKTIGI IGLGEIGSAV ARRARAFDMD VLYTGPNRKE
     EKEREIGAKY VDLDTLLKNA DFITINAAYN PKMHHLIDTE QFKMMKSTAY LINASRGPIV
     HEQALVQALK NNEIEGAALD VYEFEPDITD DLKSLNNVVL TPHIGNATFE ARDMMSKIVA
     NAAISAVQGE KPQFVVN