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Database: UniProt
Entry: U1I2F7_ENDPU
LinkDB: U1I2F7_ENDPU
Original site: U1I2F7_ENDPU 
ID   U1I2F7_ENDPU            Unreviewed;       457 AA.
AC   U1I2F7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=EPUS_01462 {ECO:0000313|EMBL:ERF76129.1};
OS   Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX   NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF76129.1, ECO:0000313|Proteomes:UP000019373};
RN   [1] {ECO:0000313|Proteomes:UP000019373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX   PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA   Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA   Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT   "Genome characteristics reveal the impact of lichenization on lichen-
RT   forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL   BMC Genomics 15:34-34(2014).
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         Evidence={ECO:0000256|ARBA:ARBA00001463};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC       ECO:0000256|RuleBase:RU004417}.
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DR   EMBL; KE720780; ERF76129.1; -; Genomic_DNA.
DR   RefSeq; XP_007786595.1; XM_007788405.1.
DR   AlphaFoldDB; U1I2F7; -.
DR   GeneID; 19236519; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   HOGENOM; CLU_025763_2_1_1; -.
DR   OMA; PCFAAFP; -.
DR   OrthoDB; 45283at2759; -.
DR   Proteomes; UP000019373; Unassembled WGS sequence.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   PANTHER; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
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; 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|PIRSR:PIRSR000185-2};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019373}.
FT   DOMAIN          190..454
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         197
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         231
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            154
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   457 AA;  49929 MW;  E6425D3F268B9484 CRC64;
     MSNLAPEPEF EQAYKELVST LENSSLFQKK PEYKKALMVV SIPERVIQFR VVWENDKGEV
     QVNRGYRVQF NSALGPYKGG LRFHPTVNLS ILKFLGFEQI FKNALTGLNM GGGKGGADFD
     PKGKSDGEIR KFCFAFMTEL SKHISANIDI PAGDIGVSPR EIGWMFGCYK KQTKLWEGVL
     TGKGGDWGGS LIRPEATGFG LVYYVQHMIQ FASDGKESFS GKKVAISGSG NVAQYAALKC
     IELGATVVSL SDSKGALIAT DEKGIQPEEI SIIAQLKVDR KQLSELANDA NFKGKYKYIE
     GVRPWLQVGD VDVALPCATQ NEVSGEEAEG LIKANCKFIA EGSNMGCTQD AIDIFEEHRK
     EKKHEAIWYA PGKAANAGGV AVSGLEMAQN SARLSWTSEE VDGRLKLIME SCFKNGLATA
     QEYIEPKEGE FPSLVAGSNI AGFIKVADAM KCHGDWW
//
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