ID   A0A0A1TBD5_9HYPO        Unreviewed;      1052 AA.
AC   A0A0A1TBD5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE            EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN   ORFNames=VHEMI07777 {ECO:0000313|EMBL:CEJ92104.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ92104.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ92104.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
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; CDHN01000004; CEJ92104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1TBD5; -.
DR   STRING; 1531966.A0A0A1TBD5; -.
DR   HOGENOM; CLU_005220_0_0_1; -.
DR   OrthoDB; 89313at2759; -.
DR   Proteomes; UP000039046; Unassembled WGS sequence.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRNR:PIRNR000184};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039046}.
FT   DOMAIN          670..934
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   REGION          14..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1052 AA;  118157 MW;  765208F1C2F80557 CRC64;
     MSAVNNVKGE AVLRPSSVPT SGTTTPNHGH RASRSALVGY VAPEFSGKAE QKKAVKALIL
     ESNWVPESLV DEQIHWFYDL LGIDDVYFKI EKPEVIARQI MSLYAAKIAA FSREDKREEI
     RLEMEADDHA IYIDTSEPGQ SNVDGPRYEG RLEAKYMDHD DNTQYRVETF RSPAVIGASP
     NSKASVRCYF VYQCQFPQRA EAIDPKETNM ELISDVGFWQ KATDNTKQIY QEIIELAVNR
     TGPVIEVFDI DDSVEKRLVI AFRTRTARGM FSSLSDLYHY YGVTSSRKYV EQFANGITVM
     SIYLRPAAPE DGYFPPMEES IVQITKEISL LYCLPQNRFA NAFAYGELSL QEAVYAHSAW
     VFVQHFLNRL GPEYVSLSQI LDINESGQAT LLSKLKRRLR TETFTPDYIL EIIKSYPALV
     RSLYASFANV HLGIPADDVV SPTPKVEVLS DEKLGETIAK TVANEHEEMV MTAFRVFNKA
     ILKTNYFTPT KVALSFRLDP SFLPEAEYPR PLYGMFLVIG AESRGFHLRF KDIARGGIRI
     VKSRSKEAYG INARNLFDEN YGLASTQQRK NKDIPEGGSK GVILLDPGQQ DKATEAFEKY
     IDSILDLLLP AETPGIKNPV VDLYGKEEIL FMGPDENTAD LVDWATEHAR IRGAPWWKSF
     FTGKSPKLGG IPHDKYGMTT LSVREYVKGI YRKLDLDPSK VRKMQTGGPD GDLGSNEILL
     GNETWTAIVD GSGVLADPNG LDREELLRLA KKRAMISEYD MSKISKDGYR VLCEDNNVTL
     PNGESVANGT SFRNTYHLRD TGMTDCFVPC GGRPESIDLI SVNRLIKDGK TTIPYIVEGA
     NLFITQDAKL RLEAAGCILY KDASANKGGV TSSSLEVLAS LAFDDENFLT HMCVNSKGEA
     PQFYQDYVRE VQAKICDNAR LEFEAIWREH ERTGEPRSIL SDKLSVAITE LDEKLQQSDL
     WTNETIRYGI LKDALPQLLL KEIGLKTMVE RIPESYLRSI FGSYLASRFV YEYGAEPSQF
     AFFDFMSQRM AAITGSTDGT ERLRRASVSG RN
//