ID   A0A401GS99_9APHY        Unreviewed;      1056 AA.
AC   A0A401GS99;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE            EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN   ORFNames=SCP_0702720 {ECO:0000313|EMBL:GBE85086.1};
OS   Sparassis crispa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Sparassidaceae; Sparassis.
OX   NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE85086.1, ECO:0000313|Proteomes:UP000287166};
RN   [1] {ECO:0000313|EMBL:GBE85086.1, ECO:0000313|Proteomes:UP000287166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA   Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT   "Genome sequence of the cauliflower mushroom Sparassis crispa
RT   (Hanabiratake) and its association with beneficial usage.";
RL   Sci. Rep. 8:16053-16053(2018).
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:GBE85086.1}.
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DR   EMBL; BFAD01000007; GBE85086.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401GS99; -.
DR   STRING; 139825.A0A401GS99; -.
DR   InParanoid; A0A401GS99; -.
DR   OrthoDB; 89313at2759; -.
DR   Proteomes; UP000287166; 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:UP000287166}.
FT   DOMAIN          695..957
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1056 AA;  117842 MW;  184A2DF1211EA0B2 CRC64;
     MASPTGSTPS IRTPTPLLGS DPANAHLLVP GHLPRTGSEQ SMQRLKNVPG YTTPVFKGKD
     EQRAKVHANV VAKGFIPREL VANEVNWFYS HLGIDDTYFQ AESVDVISDH IIALFGAKVL
     AYTKHDPSQL VIDLEKIDEN GNGATFIHTS SPGKTATEGP GASCENRIDA LYLDNSTPSK
     AYRLETYRSQ GLVSATASQQ LRCYFITKCN FPASPPPSTR TDGKTDIRTV SDPVFLEKAS
     ENTLEIYQNV MWNVETRYGP VIEVFEVEGS RERRLVIGYK MGGTSKFFSA LSNLYHFYAL
     YSARKYVEQF SNGITIISLY LNPLPSALNA PPIEHSIFQV MKEASLLYCL PDNPFFYAEP
     GQNGGHAVQE ATYAYCGWVF AQHFCNRLGP AYLALKNILD ESNPSHAEVL NDIKRRFREE
     TFTRESIAQV IHAHADLINL LYVNFAMVHY PAADEASQLM PTLSYQRLQT QVPLSDEDLY
     DKIRKTVHNK HELQVLESFL IFNKHVLKTN FYQPTKVALS FRLAPDFLPE VEYPKKPFGM
     FFIIGGEFRG FHIRFRDVAR GGIRIVMSRN RENYSINQRM LFDENYGLAS TQSLKNKDIP
     EGGAKGTILP SLGSSPRLCF EKYVDAVIDL LIPGQSPGIK ERLIDLYGKP ELLFFGPDEG
     TADMMDWAAL HARARGAETW WKSFTTGKSA ETLGGIPHDQ FGMTSLSIRQ YVLGIYKQLG
     LREKDITKVQ TGGPDGDLGS NEILLSSDKT IAVIDGSGVL ADPAGIDREE LIRLAKLRVP
     VAHFDKSKLS KDGYLVRVED QDLKLPSGEV ILDGTDFRNG AHLRFKADLF VPCGGRPEAV
     NISNVAALVD SEGKPHFKYI VEGANLFLTQ QARLYLEKRK VVVFKDSSTN KGGVTSSSLE
     VLAGLALSTQ EYVDLMIFKD GKPSRFYQSY VRDIQAKVTE NALAEFQCLW REHARAQGAK
     ARTLISDELS ITLNDLQTEL EGSDLYEDPA CRRGVMSQAV PKMLVDEVGL DTVLNRLPEP
     YQRALFSSWM ASHFIYKYGV NGSSVDFFHF VRDLAA
//