DHE2_STAAS
ID DHE2_STAAS Reviewed; 414 AA.
AC Q6GAW8;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=NAD-specific glutamate dehydrogenase;
DE Short=NAD-GDH;
DE EC=1.4.1.2;
GN Name=gluD; OrderedLocusNames=SAS0828;
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 -!- 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; BX571857; CAG42603.1; -; Genomic_DNA.
DR RefSeq; WP_000138487.1; NC_002953.3.
DR AlphaFoldDB; Q6GAW8; -.
DR SMR; Q6GAW8; -.
DR GeneID; 66839156; -.
DR KEGG; sas:SAS0828; -.
DR HOGENOM; CLU_025763_1_2_9; -.
DR OMA; WLQNRNG; -.
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 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..414
FT /note="NAD-specific glutamate dehydrogenase"
FT /id="PRO_0000223330"
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