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
//