ID   A0A2S4KS72_9HYPO        Unreviewed;      1071 AA.
AC   A0A2S4KS72;
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=TPAR_06793 {ECO:0000313|EMBL:POR33018.1};
OS   Tolypocladium paradoxum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX   NCBI_TaxID=94208 {ECO:0000313|EMBL:POR33018.1, ECO:0000313|Proteomes:UP000237481};
RN   [1] {ECO:0000313|EMBL:POR33018.1, ECO:0000313|Proteomes:UP000237481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRBC 100945 {ECO:0000313|EMBL:POR33018.1,
RC   ECO:0000313|Proteomes:UP000237481};
RA   Quandt C.A., Patterson W., Spatafora J.W.;
RT   "Harnessing the power of phylogenomics to disentangle the directionality
RT   and signatures of interkingdom host jumping in the parasitic fungal genus
RT   Tolypocladium.";
RL   Submitted (JAN-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:POR33018.1}.
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DR   EMBL; PKSG01000756; POR33018.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4KS72; -.
DR   STRING; 94208.A0A2S4KS72; -.
DR   OrthoDB; 89313at2759; -.
DR   Proteomes; UP000237481; 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:UP000237481}.
FT   DOMAIN          686..951
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   REGION          18..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1071 AA;  119875 MW;  129BE87619A7794F CRC64;
     MSSALPKPKP LANLQFEEAS RGPSPQPTHF SVPLVSHSNG NGNRTLRSAT VGYVAPEFTG
     KLEQMKTVKD IIVRGGWIPE SLVEDQIRWF YEQLGIDDAY FRIETPDVIA SQITSLYAAK
     VAAYSREDKR EEIRLDMEAN DHAIYIDTSE PGKGHVSGPR YESRLEAKYL DHQGKTKYRV
     ETFRSPAVIG ASPSSKASLR CYFVYQCQFK HRPEETNPKE TNIELISDSG FWQKATDNTK
     QIYQEIIELA VTRTGPVIEI FDIEGVAEKR LVVAFRTRTA RGMFSALSDL YHYYGVTSSR
     KYVEQFSNGI TVMSIYLKPA NLSDGYFPPI EESIHQITKE ISLLYCLPQN KFHNLFAVGD
     LSLQEAVYAH SAWVFVQHFL NRLGPEYASL SEILSSADTA QAALLSKLKR RLRTETFTPD
     YILEIIQNYP GLVRSLYASF ANIHLGGGPD LDQQAVAPTP VVEVLSDARL QETIAKTVSN
     EHDEMVMTAF RVFNNAILKT NYFTPTKVAL SFRLDPSFLP EVEYPRRLYG MFLVIGAESR
     GFHLRFRDIS RGGIRIVKSR SKEAYGINAR NLFDENYGLA STQQRKNKDI PEGGSKGVIL
     LDPKQQDKAQ EAFEKYIDSI LDLLLPAASP GIKNKLVDLY GKEEILFMGP DENTADLVDW
     ATEHARARGA PWWKSFFTGK SQKLGGIPHD KYGMTTLSVR EYVKGIYRKL ELDPSTVRKM
     QTGGPDGDLG SNEILLGNEK WTAIVDGSGV LADPNGLDRD ELLRLAKKRA MIIEYDMSKL
     SKDGYRILCE ENNVTLPSGE VVTNGTSFRN TYHLRDTGMT DAFVPCGGRP ESIDLISVNR
     LIKDGKTTIP YIVEGANLFI TQDAKLRLEA AGCILYKDAS ANKGGVTSSS LEVLASLSFD
     DEGFVENMCV DAKTGEAPPF YNDYVREVQA KIRENARLEF EAVWREHEAT GTPRSILSDK
     LSIAITDLDE ELQKSDLWAN RTIRYAVLGD ALPALLLQKI GLDTIISRVP DSYLRSIFGS
     YLASRFVYEF GSEPSQFAFF DFMSKRMAKI TGRSDGSEQI RRMSMSGGAG L
//