ID   E6ZVU8_SPORE            Unreviewed;      1051 AA.
AC   E6ZVU8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE            EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN   ORFNames=sr16604 {ECO:0000313|EMBL:CBQ71255.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ71255.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ71255.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
CC   -!- FUNCTION: NAD(+)-dependent glutamate dehydrogenase which degrades
CC       glutamate to ammonia and alpha-ketoglutarate.
CC       {ECO:0000256|PIRNR:PIRNR000184}.
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         Evidence={ECO:0000256|PIRNR:PIRNR000184};
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000184}.
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DR   EMBL; FQ311443; CBQ71255.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZVU8; -.
DR   EnsemblFungi; CBQ71255; CBQ71255; sr16604.
DR   VEuPathDB; FungiDB:sr16604; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   HOGENOM; CLU_005220_0_0_1; -.
DR   OrthoDB; 89313at2759; -.
DR   Proteomes; UP000008867; Chromosome 21.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016210; NAD-GDH_euk.
DR   PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF42; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   PIRSF; PIRSF000184; GDH_NAD; 1.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRNR:PIRNR000184};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184}.
FT   DOMAIN          683..945
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   1051 AA;  117149 MW;  995FE71A4E946F06 CRC64;
     MAPSIDQQSS SLGDVSKLKS ALLSATSANS RSGSHTPIDH VIANNAGYTD TVFEGKADQA
     AQVKQLLSSK GFIPPDLVTA EVDWFYQNLG IDDTYFALES VETVADHILA LFGAKIMAYT
     KHSNSLEIDL EKESENGAVF IHSSQAGKSQ AQGPQWERRI DANYLDKSSV DKAYRLETYR
     SAGSVSAQSQ QQLRCYFLAK CNFVEPRPAP DSPSYADIRA VSDRTFLTKA SDNTLDIYQS
     IMDEVLRRQG PVIEMFEVEG SRERRIVIGY RMGTTNSFFS ALSDLYHFYG LFSSRKYVEQ
     FSNNVTIISI YLNPLPASNS PPIEHSIHQV MKEASLIYVL PDNPFFQPAL AENTHAVQEA
     TYAYVGWLFA QHFCNRLGQA YQALRNVLNE NDSQQAAILN EIKLRFREET FTRQSIQEVI
     ENHPTLIRLL YVHFANIHYP GGADDQELVP TLSYQRLVKE EVLDDNQMYD RIRKAANNTH
     ERQVLEAFLF FNKAVLKTNF YTPTKVALSF RLDPGFLPEV EYPVKPYGII FVVGAEFRGF
     HVRFRDVARG GIRIVRSRNR ENYSINQRTL FDENYALAST QHLKNKEIPE GGAKGTILPT
     LDANPKLAFE KYVDAILDLL IKGQTPGVKE EIVDLLGKEE ILFLGPDEGT ADLMDFAAEH
     ARARGAPWWK SFTTGKTAAT LGGVPHDVWG MTSLSVRQYI IGIYRMLGLK EQEVTKVQTG
     GPDGDLGSNE ILLSVDKTVA IIDGSGVIYD PVGLNRQELV RLAKARKMIS DFDASKLSSN
     GYRVLVEQND VKLPSGEVVP DGVAFRNSAH LRFKADLFVP CGGRPEAINI SNVNQLFDQD
     GKPHFKYIVE GANLFITRQA RLELEKRGVI LYPDASANKG GVTSSSLEVL CGLSLEDAEY
     VESMLFKDGK PTNFYLSYVR DIQTIIGRNA RAEFEAIWRE NLETGKPRST ISTELSTTLN
     KLSEELEATD LFSNEQLRSA VLGQVFPPTL IKKVGLPKLI ERIPEAYARS AFAAKVAASF
     VYANGPNASH VDFYKHISTL LAQPSPAAAQ Q
//