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Database: UniProt
Entry: W0J7Y2_9BACT
LinkDB: W0J7Y2_9BACT
Original site: W0J7Y2_9BACT 
ID   W0J7Y2_9BACT            Unreviewed;       447 AA.
AC   W0J7Y2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=OPIT5_25725 {ECO:0000313|EMBL:AHF93108.1};
OS   Opitutaceae bacterium TAV5.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX   NCBI_TaxID=794903 {ECO:0000313|EMBL:AHF93108.1, ECO:0000313|Proteomes:UP000003813};
RN   [1] {ECO:0000313|EMBL:AHF93108.1, ECO:0000313|Proteomes:UP000003813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAV5 {ECO:0000313|EMBL:AHF93108.1};
RX   PubMed=25744998;
RA   Kotak M., Isanapong J., Goodwin L., Bruce D., Chen A., Han C.S.,
RA   Huntemann M., Ivanova N., Land M.L., Nolan M., Pati A., Woyke T.,
RA   Rodrigues J.L.;
RT   "Complete Genome Sequence of the Opitutaceae Bacterium Strain TAV5, a
RT   Potential Facultative Methylotroph of the Wood-Feeding Termite
RT   Reticulitermes flavipes.";
RL   Genome Announc. 3:0-0(2015).
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; CP007053; AHF93108.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0J7Y2; -.
DR   STRING; 794903.OPIT5_25725; -.
DR   KEGG; obt:OPIT5_25725; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_2_1_0; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000003813; Chromosome.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
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   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003813}.
FT   DOMAIN          203..445
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        127
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         210
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         241
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            167
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   447 AA;  49031 MW;  19D24426D1984023 CRC64;
     MSDQSLDSFL ARIRQRDPVQ PEFHQAVEEF FRSLWPFLKH HPKYAKAGIL DRLVEPERVI
     MFRVPWVDDT GVVHVNRGFR VQMSSAIGPY KGGIRFHPSV NLGILKFLAF EQVFKNSLTT
     LPMGGGKGGS DFDPKGKSEN EIMRFCQSFM TELCRHIGAD VDVPAGDIGV GGREVGYMFG
     QYKRLTNQFT SVLTGKGLAF GGSLIRPEAT GYGCVYFAQE MMQRARLGFE GKRVAVSGSG
     NVAQYAAEKV IEFGGKVVSF SDSNGTVEIP AGMTDEQLKW AMDLKNNRRG RIEAFAQHFK
     LPYHADKRPW HIACDIALPC ATQNEVDGED AKVLVRNGCK CVAEGANMPS TLEAVDVFVG
     NRILYGPGKA ANAGGVATSG LEMSQNAMRL SWSRGEVDDR LHAIMQNIHH VCVEHGTEQD
     GFVNYVNGAN IGGFVKVADA MLAQGIV
//
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