ID A0A0U1LQ43_TALIS Unreviewed; 1090 AA.
AC A0A0U1LQ43;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=PISL3812_01897 {ECO:0000313|EMBL:CRG84640.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG84640.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG84640.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG84640.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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; CVMT01000001; CRG84640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1LQ43; -.
DR STRING; 28573.A0A0U1LQ43; -.
DR OMA; LYCLPQN; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000054383; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054383}.
FT DOMAIN 723..987
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1090 AA; 123035 MW; F2A4BB5A6B003BA4 CRC64;
MSIDPGSAHP PSEGLPSPAV GGLSTPQLVL DSGSSGPGTP IGFQRYPHNK HLDNVTRTPG
RQPSPQPTHL ALPGHHRVLP EEGTGYIPSK FEGKQKQMEE VMDRLEEKGF FPSDFVISET
TWFYNMLGID DMYFQTESVE SIVTQILSLY AAKVAAYARD DKRLEIRLDK EDEDHAVYID
TSKPGVTSFS GPNYESRIDA KYIDGSRPGV SYRVESFRST SPLPGETEQQ LRCYFVYKCQ
FANPNPSPEE TNIDIIGEKR FLQKATPNTK AIYREIITTA VSRTGPVIEI YDIEGTREKR
LVVAYRQGSA MGIFSALSDL YHYYRLTSSR KYLESFSNGI NVISLYLRPI PNPEISQKHP
PIEAAIHQIM KEVSLLYCIP RNRFQNHFAS GRLSLQETIY SHCAWIFIQQ FLNRLGSEYT
SLTALLDSNN SVHAELLSKI KKRLRTETFT SDYISEIISK YPELIHKLYL DFANTHYVQT
GHPEDDFLPT LSYLRLQVDE ILDDAGLKAL IAKTVVNEHD EMVMMAFRIF NKAVLKTNFY
TSTKVGLSFR LNPNFLPEHE YPQRLYGMFL VISSEFRGFH LRFRDIARGG IRIVKSRNKE
AYGINARSLF DENYNLANTQ QRKNKDIPEG GAKGVILLDV EHQDKARVAF EKYIDSILDL
LIAPTSPGIK DPIVDLHGKD EILFMGPDEN TADLVDWATE HARKRGAAWW KSFFTGKSPK
LGGIPHDAYG MTTLSVRQYV LGIYRKLKID PSTVKKLQTG GPDGDLGSNE ILLGNEQYTA
IVDGSGVIVD PNGLDRDELV KLAKNRVMIS HFDLSKLSSE GYRVLVEDTN VKLPSGETVH
NGMVFRNKFH LRSNQSLDLF VPCGGRPESI DLSTVGKLIV NGKSVIPYIV EGANLFITQD
AKLRLEKAGC ILYKDASANK GGVTSSSLEV LASLSLDDKE FVENMCVHED GTVPEFYQTY
VKEVQEVIKR NAMLEFEAIW REHEQTGLLR SVLSDRLSLA ITGLDEELQK TSLWDNTELR
HTVLQKALPR LLLEKVGLET ILQRVPENYL KSIFGSYLAS RFVYEYGSSP SQFAFFDFMS
KNFSHQMLPK
//
