ID A0A364Y8Z1_9BACT Unreviewed; 424 AA.
AC A0A364Y8Z1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=DQQ10_05000 {ECO:0000313|EMBL:RAW03447.1};
OS Pseudochryseolinea flava.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Pseudochryseolinea.
OX NCBI_TaxID=2059302 {ECO:0000313|EMBL:RAW03447.1, ECO:0000313|Proteomes:UP000251889};
RN [1] {ECO:0000313|EMBL:RAW03447.1, ECO:0000313|Proteomes:UP000251889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDU1-6 {ECO:0000313|EMBL:RAW03447.1,
RC ECO:0000313|Proteomes:UP000251889};
RA Li Y., Wang J.;
RT "Chryseolinea flavus sp. nov., a member of the phylum Bacteroidetes
RT isolated from soil.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RAW03447.1}.
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DR EMBL; QMFY01000001; RAW03447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364Y8Z1; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000251889; Unassembled WGS sequence.
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; 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:UP000251889}.
FT DOMAIN 191..422
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 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 358
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 424 AA; 46371 MW; 4F88D7718DE04CB5 CRC64;
MAYIEPAPLK DKENPFEAMM SRFKVASQIL GLEEEIYNVL KNPARQVIVS LPVTMDDGTI
KVFEGYRVIH STILGPSKGG IRFDMAVNLD EVKALAAWMT WKCAVVDIPY GGAKGGVACN
PREMSAGEIE RLMRAYTQAM ADVFGPDQDI PAPDMGTGPR EMAWLMDQYS RIQGMTTHAV
VTGKPLVMGG SLGRTEATGR GVMVTAMAAM EKLKINPYKA TCAVQGFGNV GSWAARLLHE
RGLIVQAVSD LSGAYYNEKG IEIDKAVQYR DNNKGSLEGF AGAEKISNED LLTLPVDLLV
PAATEDVINS TNAPNIKAKL IVEGANGPTS SKADNVINEK GIMVVPDILA NAGGVTVSYF
EWVQNRLGYK WTADRVNRRS DRIMKDAFNN VYRVSQEYKV PMRIAAYMVA IDKVSKTYKF
RGGY
//
