GenomeNet

Database: UniProt
Entry: R9AH60_WALI9
LinkDB: R9AH60_WALI9
Original site: R9AH60_WALI9 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system