ID   DHE2_STAAN              Reviewed;         414 AA.
AC   Q7A6H8;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=NAD-specific glutamate dehydrogenase;
DE            Short=NAD-GDH;
DE            EC=1.4.1.2;
GN   Name=gluD; Synonyms=gudB; OrderedLocusNames=SA0819;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=N315;
RX   PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA   Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA   Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA   Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT   "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT   aureus during the post-exponential phase of growth.";
RL   J. Microbiol. Methods 60:247-257(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC         NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; BA000018; BAB42058.1; -; Genomic_DNA.
DR   PIR; G89862; G89862.
DR   RefSeq; WP_000138487.1; NC_002745.2.
DR   AlphaFoldDB; Q7A6H8; -.
DR   SMR; Q7A6H8; -.
DR   SWISS-2DPAGE; Q7A6H8; -.
DR   EnsemblBacteria; BAB42058; BAB42058; BAB42058.
DR   GeneID; 66839156; -.
DR   KEGG; sau:SA0819; -.
DR   HOGENOM; CLU_025763_1_2_9; -.
DR   OMA; WLQNRNG; -.
DR   Proteomes; UP000000751; Chromosome.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; ISS:UniProtKB.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..414
FT                   /note="NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000223328"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            146
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
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