ID   DHE4_LACBS              Reviewed;         450 AA.
AC   P54388; B0CZ97;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4;
DE   AltName: Full=NADP-dependent glutamate dehydrogenase;
GN   Name=GDHA; ORFNames=LACBIDRAFT_292653;
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX   NCBI_TaxID=486041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lorillou S.S., Martin F.F.;
RT   "Cloning, sequence analysis and expression of a cDNA encoding NADP-
RT   glutamate dehydrogenase from the ectomycorrhizal basidiomycete Laccaria
RT   bicolor.";
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686;
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC         NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.4;
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; U31369; AAA82936.1; -; mRNA.
DR   EMBL; DS547094; EDR12114.1; -; Genomic_DNA.
DR   RefSeq; XP_001876378.1; XM_001876343.1.
DR   AlphaFoldDB; P54388; -.
DR   SMR; P54388; -.
DR   STRING; 486041.P54388; -.
DR   EnsemblFungi; EDR12114; EDR12114; LACBIDRAFT_292653.
DR   GeneID; 6072874; -.
DR   KEGG; lbc:LACBIDRAFT_292653; -.
DR   HOGENOM; CLU_025763_2_1_1; -.
DR   InParanoid; P54388; -.
DR   OrthoDB; 692851at2759; -.
DR   BRENDA; 1.4.1.4; 2839.
DR   Proteomes; UP000001194; Unassembled WGS sequence.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..450
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182789"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   CONFLICT        17
FT                   /note="Q -> P (in Ref. 1; AAA82936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="E -> G (in Ref. 1; AAA82936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        38
FT                   /note="Q -> P (in Ref. 1; AAA82936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="V -> I (in Ref. 1; AAA82936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="A -> G (in Ref. 1; AAA82936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        349
FT                   /note="A -> E (in Ref. 1; AAA82936)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  48550 MW;  8FDA699CA3D46945 CRC64;
     MVLPVEPEYE QALSELQNSL KPFLAANPDY EKALEIVQIP ERVLQFRVVW EDDQGKAQVN
     RGFRVQYNSA LGPYKGGLRL HPSVNLSILK FLGFEQTFKN ALTGLSMGGG KGGSDFDPKG
     KSDGEIRRFC TSFMSELFRH IGQDTDVPAG DIGTGAREIG YLFGAYKKLQ NEFVGMLTGK
     GLAWGGSFIR PEATGYGLIY YVEHMIAKAA PEYSLSKPET LVAISGSGNV AQFTALKVIE
     LGATVLSLSD SKGSLIAEKG YTKEFIKEIG QLKLKGGALE SLAQREGYTY HAGKRPWSLL
     PVVHVALPGA TQNEVSKTEA EDLIKAGVRI VAEGSNMGCT EDAIAVFEAS RKAGAGGVWY
     APGKASNCGG VAVSGLEMAQ NSQRLAWTTD QVDQKLKKIM AECYEICLSA GTKWSGEEIK
     DGVLPSLLSG ANVAGFIKVA DAMREHGDWW