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Database: UniProt
Entry: Q6G716
LinkDB: Q6G716
Original site: Q6G716 
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   05-DEC-2018, entry version 87.
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.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence 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}.
DR   EMBL; BX571857; CAG44007.1; -; Genomic_DNA.
DR   RefSeq; WP_000417016.1; NC_002953.3.
DR   ProteinModelPortal; Q6G716; -.
DR   SMR; Q6G716; -.
DR   KEGG; sas:SAS2196; -.
DR   HOGENOM; HOG000136700; -.
DR   OMA; KWIAHNG; -.
DR   BioCyc; SAUR282459:G1G3P-2463-MONOMER; -.
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       Putative 2-hydroxyacid dehydrogenase
FT                                SAS2196.
FT                                /FTId=PRO_0000312187.
FT   NP_BIND     155    156       NAD. {ECO:0000250}.
FT   NP_BIND     234    236       NAD. {ECO:0000250}.
FT   NP_BIND     283    286       NAD. {ECO:0000250}.
FT   ACT_SITE    236    236       {ECO:0000250}.
FT   ACT_SITE    265    265       {ECO:0000250}.
FT   ACT_SITE    283    283       Proton donor. {ECO:0000250}.
FT   BINDING     260    260       NAD. {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
//
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