ID A0A2T4CJZ3_TRILO Unreviewed; 1067 AA.
AC A0A2T4CJZ3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=M440DRAFT_16127 {ECO:0000313|EMBL:PTB81828.1};
OS Trichoderma longibrachiatum ATCC 18648.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB81828.1, ECO:0000313|Proteomes:UP000240760};
RN [1] {ECO:0000313|EMBL:PTB81828.1, ECO:0000313|Proteomes:UP000240760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB81828.1,
RC ECO:0000313|Proteomes:UP000240760};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) 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; KZ679126; PTB81828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4CJZ3; -.
DR STRING; 983965.A0A2T4CJZ3; -.
DR Proteomes; UP000240760; 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:UP000240760}.
FT DOMAIN 686..951
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 119713 MW; 3CDD17F9530E3FE0 CRC64;
MASSTPPKPK TLAQIRSAES DSSRGPSPQP THVSVPPVPL ALRNGHRVLR SATVGYVAPQ
FEGKTEQIKA VKSIIQQGGW LPENLIDEQI EWFYEKLGID DVYFHIETPE VIANQITSLY
AAKVAAHSRE DKHEEIRLDM EAHDHAIYID TSEPGKAHVS GPRYESRLES KYLDHQGKSK
YRVETFRSPA AIGASPNSKA TVRCYFVYQC HFKQSPESTD PKETRIEVIS DVGFWQKATA
NTKQVYQEII EIAVNRAGPV IEVFDIEGSA EKRLVVAFRS RTARGIFSTL SDLYHYYGVT
SSRKYVEQFS NGITVMSAYL RPAPNLDGYF PSIETSIHQI TKEISLLYCL PQNKFHHLFA
TGELSLQESV YAHSAWVFVQ HFLNRLGPEY ASLLEILDPK QNAHAALLSK LKRRLRTETF
TPDYILEIIQ SYPELVRLLY ASFASVHLGV QDSNVLLATP AVEVLSDEKL RDKISKTVAN
EHDEMVMTAF RVFNNAILKT NYFTPTKVAL SFRLDPSFLP EAEYPKPLYG MFLVIGAESR
GFHLRFRDIS RGGIRIVKSR SKEAYGINAR NLFDENYGLA STQQRKNKDI PEGGSKGVIL
LDPKQQDKAT EAFEKYIDSI LDLLLPAETP GIKNPIVDLY GKQEILFMGP DENTADLVDW
ATEHAKARGA PWWKSFFTGK SPKLGGIPHD KYGMTTLSVR EYVKGIYRKL DLDPSQVRKM
QTGGPDGDLG SNEILLSNEK YTAVVDGSGV LADPNGLDKD ELIRLARKRV MISEYDLSKL
SKDGYRVLCD ENNVTLPSGE VVNNGTSFRN TYHLRETNTT DCFVPCGGRP ESIDLISVNR
LIKEGKSIIP YIVEGANLFI TQDAKLRLES AGAILYKDAS ANKGGVTSSS LEVLASLSFD
TEGFIENMCV DPKTGKAPQF YDDYVREVQS KIQENARLEF EAIWREHEQT GIARSILSDK
LSGAITDLDE KLQHSDLWEN ETIRKGVLRE ALPKMLLNKI GLDTIISRVP ENYLRAIFGS
YLASRFVYEF GSEPSQFAFF DFMSKKLADI SGQANGAEQV RRMSISQ
//
