ID   Y2196_STAAS             Reviewed;         317 AA.
AC   Q6G716;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase SAS2196;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=SAS2196;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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; BX571857; CAG44007.1; -; Genomic_DNA.
DR   RefSeq; WP_000417016.1; NC_002953.3.
DR   AlphaFoldDB; Q6G716; -.
DR   SMR; Q6G716; -.
DR   KEGG; sas:SAS2196; -.
DR   HOGENOM; CLU_019796_1_2_9; -.
DR   OMA; KMKPNCI; -.
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 SAS2196"
FT                   /id="PRO_0000312187"
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;  4D87D9BDA5DCD2B5 CRC64;
     MEKVYVAGAI PEVGLKLLQE HFEVEMYEGK GLVDKDTLIK GVKNATALIS LLSTNVDKDV
     IDAGKDLKII ANYGAGFNNI DIEYAREKSI DVTNTPKAST NATADLTIGL VLAVARRIVE
     GDQLSRTTGF DGWAPLFFRG REVSGKTIGI IGLGEIGSAV ARRARAFDMD VLYTGPNRKE
     EKEREIGAKY VDLDTLLKNA DFITINAAYN PKMHHLIDTE QFKMMKSTAY LINASRGPIV
     HEQALVQALK DNEIEGAALD VYEFEPDITD DLKSLNNVVL TPHIGNATFE ARDMMSKIVA
     NAAISAVQGE KPQFVVN