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Database: UniProt
Entry: V5A664_9ARCH
LinkDB: V5A664_9ARCH
Original site: V5A664_9ARCH 
ID   V5A664_9ARCH            Unreviewed;       418 AA.
AC   V5A664;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=A07HR60_02200 {ECO:0000313|EMBL:ESS11055.1};
OS   uncultured archaeon A07HR60.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=1412874 {ECO:0000313|EMBL:ESS11055.1, ECO:0000313|Proteomes:UP000030679};
RN   [1] {ECO:0000313|Proteomes:UP000030679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24335829;
RA   Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA   Heidelberg K.B., Banfield J.F., Allen E.E.;
RT   "Seasonal fluctuations in ionic concentrations drive microbial succession
RT   in a hypersaline lake community.";
RL   ISME J. 0:0-0(2013).
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; KI543233; ESS11055.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5A664; -.
DR   STRING; 1412874.A07HR60_02200; -.
DR   PATRIC; fig|1412874.3.peg.2535; -.
DR   Proteomes; UP000030679; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
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; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 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:UP000030679}.
FT   DOMAIN          183..415
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         221
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            146
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   418 AA;  44938 MW;  4481A3FFFA7B1B43 CRC64;
     MSEETNPFES LQEQIEDASA YVDIGDDVIE RLKRPERVLE TTLTVELDDG GLKTFAGYRS
     QFNGDRGPYK GGIRYHPGVN RAEVKALSGW MVYKCALVDI PFGGGKGGIE VDPAAHSASE
     MERLTRAFAA ELRPLIGVDR DIPAPDVNTG QQEMNWIKDT YETLERTTEP GVITGKAPGS
     GGSEGRVRAT GRSVMFSTRE TLEWLGRELE GATVAVQGYG NAGSVAAQEL DKQGATVVAA
     SDSSGAIYNP SGFDTVAAKQ YKTETGSLSG FEGATEEISN EDLLTLDVDV LIPAALENAI
     DESLATDVRA DLIVEAANGP LTPGADEVLT DTDTYVVPDI LANAGGVTVS YFEWVQNRGR
     FYWPESRVNN ELETVITDAF DGLVAAFDEQ DLPSLRMAAY VVSLRRVAGA FRQGGNFP
//
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