ID R9AH60_WALI9 Unreviewed; 1065 AA.
AC R9AH60;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=J056_001931 {ECO:0000313|EMBL:EOQ99375.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOQ99375.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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; KE007242; EOQ99375.1; -; Genomic_DNA.
DR RefSeq; XP_009269834.1; XM_009271559.1.
DR AlphaFoldDB; R9AH60; -.
DR STRING; 1299270.R9AH60; -.
DR GeneID; 20374883; -.
DR KEGG; wic:J056_001931; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_005220_0_0_1; -.
DR OMA; LYCLPQN; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000014064; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016210; NAD-GDH_euk.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF24; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064}.
FT DOMAIN 706..968
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 119960 MW; 5FD10209BBF57893 CRC64;
MKLPEITSTG STESTESTES PFPHPRLRSS SPSPSFISFL SLRDPLLTKS QSQTPHLFIP
STPSPLQKSN SDLALNKLKN DKGYTDTIYA DKDVQCQKVI ENLKHKAFIP ENLVDNEVNW
FYTNLGIDDT YFKLETVDTI SDHIISLYAA KLVAYTKHRN DSNKLDIDLK KERENDAVFI
HSDKSGHGVE QLIDSKYFDS DSIPFRLETY TSKAKGNLRC YFLSKCNFPK LESKENDIRK
IADPLFLEKA SANTIDIYQR ILNQVDVRTG PVVEGFEIEG TTEHRIVIGY KRGTTKGFFS
TLTDLYHFYG LHSTRKFVEH FSNGSMIVSL YLNQDPLVPA PPISHSVVQI VREVSLIYCL
PDNPLFSRAA ETDPGMGNAV QEATYAYVGY IYITHFCNRL GPAYEALQSL LDESNSTHMG
VLADLKRRLR EETFTKTAIL DVIQSYPELV RLLYTQFAMA HYPASSANEE VVPTLSHQRL
QQVHVMSDEE LHATLQKGTR NPFELQVLES FMVMNKHTLK TNFYQPTKVA LSFRLDGDFL
PNNEYTQKPY GIFFIVGSDF QGFHVRFKDV ARGGIRILRS RDSENYATNQ RMLFDECYNL
SSTQSLKNKD IPEGGSKGVI LPNLNANPEL AFERYIDSII DLLIPGNSPG IKEPIVDLHA
KQEILFLGPD EGTAGYMDWA ALHARSRGAP WWKSFTTGKS ADTLGGIPHD VYGMTSRSVR
QYYVGILDKM AMDEETTTKV QTGGPDGDLG SNEILLSKDK TVAIVDGSGV IYDPVGLDRA
ELTRLAKQRV MIKEFDVSRL SKDGYRVLCE QNDVKLPSGE IVQDGTSFRN GYHLRVKADV
LIPCGGRPQA VNISNVNQLF DGEGKPHFKI IVEGANLFVT QQARLMLEKR GVILIRDSSA
NKGGVTSSSL EVLAGLALNE EEYSELMMYT NGKPSSFYES YVKDIQEIIE SNARMEFNTI
WSEYNRLGGT ESRTIISDNL SRTLNKLQLE LESSDGLFAD VEKRKKVLSK AMPKTLVQYV
GIDNLLQRLP LSYQKALFAC QISRFCYQYG PAASQVEFYL YMSQF
//