ID   DHE2_STAAR              Reviewed;         414 AA.
AC   Q6GID0;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   04-NOV-2008, entry version 30.
DE   RecName: Full=NAD-specific glutamate dehydrogenase;
DE            Short=NAD-GDH;
DE            EC=1.4.1.2;
GN   Name=gluD; OrderedLocusNames=SAR0920;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate
CC       + NH(3) + NADH.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BX571856; CAG39926.1; -; Genomic_DNA.
DR   RefSeq; YP_040342.1; -.
DR   GeneID; 2861713; -.
DR   GenomeReviews; BX571856_GR; SAR0920.
DR   KEGG; sar:SAR0920; -.
DR   HOGENOM; Q6GID0; -.
DR   BioCyc; SAUR282458:SAR0920-MON; -.
DR   GO; GO:0004352; F:glutamate dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DHase.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DHase_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DHase_dimer.
DR   InterPro; IPR014362; Glu_DHase.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11606:SF2; GLFV_DH; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    414       NAD-specific glutamate dehydrogenase.
FT                                /FTId=PRO_0000223329.
FT   ACT_SITE    106    106       By similarity.
SQ   SEQUENCE   414 AA;  45760 MW;  F79290751F6312C7 CRC64;
     MTENNNLVTS TQGIIKEALH KLGFDEGMYD LIKEPLRMLQ VRIPVRMDDG TVKTFTGYRA
     QHNDAVGPTK GGVRFHPDVD EEEVKALSMW MTLKCGIVNL PYGGGKGGIV CDPRQMSIHE
     VERLSRGYVR AISQFVGPNK DIPAPDVFTN SQIMAWMMDE YSALDKFNSP GFITGKPIVL
     GGSHGRDRST ALGVVIAIEQ AAKRRNMQIE GAKVVIQGFG NAGSFLAKFL YDLGAKIVGI
     SDAYGALHDP NGLDIDYLLD RRDSFGTVTN LFEETISNKE LFELDCDILV PAAISNQITE
     DNAHDIKASI VVEAANGPTT PEATRILTER GILLVPDVLA SAGGVTVSYF EWVQNNQGYY
     WSEEEVNEKL REKLEAAFDT IYELSQNRKI DMRLAAYIIG IKRTAEAARY RGWA
//