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Database: UniProt
Entry: A0A0Q0VPD9_9EURY
LinkDB: A0A0Q0VPD9_9EURY
Original site: A0A0Q0VPD9_9EURY 
ID   A0A0Q0VPD9_9EURY        Unreviewed;       428 AA.
AC   A0A0Q0VPD9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=APR53_06505 {ECO:0000313|EMBL:KQC05766.1};
OS   Methanoculleus sp. SDB.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=1735326 {ECO:0000313|EMBL:KQC05766.1, ECO:0000313|Proteomes:UP000051748};
RN   [1] {ECO:0000313|EMBL:KQC05766.1, ECO:0000313|Proteomes:UP000051748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDB {ECO:0000313|EMBL:KQC05766.1};
RA   Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA   Suflita J.M., Callaghan A.V.;
RT   "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing Consortium.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KQC05766.1}.
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DR   EMBL; LKUD01000004; KQC05766.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q0VPD9; -.
DR   STRING; 1735326.APR53_06505; -.
DR   Proteomes; UP000051748; 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}.
FT   DOMAIN          201..426
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        105
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         189
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         233
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         362
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            145
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   428 AA;  46882 MW;  030340C891E2B632 CRC64;
     MEEMNLLETV RKQICTCSVD LRLTPNVEAL LKKPMHELHV SLPVRMDDGT IQTFQGFRVQ
     YNNARGPAKG GIRFHPDETI NTIRGLAAIM TWKCALHDLP LGGAKGGVIC NPKTMSRGEL
     ERLSRAYMRA ICRFIGPGRD IPAPDVYTNP QVMAWMMDEY ASITGYTEFG VITGKPVTLG
     GSEGRDDATA RGGWIAIREA GKHLGIDFAI RETAAAMEMP VTDTTVAVQG FGNVGYHAAR
     LAGEMAGCRV VAVSDSRGAI YNQEGLDPDS VMEYEKKTGS VTGYPGASAM TNEELLELDV
     DILIPAALEN VITAKNASNI KAKILAEFAN GPTTREAEDI LSQNGIHIIP DFLCNGGGVI
     VSYYEMVQNY NMDHWPAAEV RRRLDDKMTA AYTAVYTMAR THSVPMRQAA YTIALQRVIR
     AMEDRGWV
//
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