ID A0A1Q3M558_9BACT Unreviewed; 310 AA.
AC A0A1Q3M558;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:OJU54536.1};
DE Flags: Fragment;
GN ORFNames=BGN96_16615 {ECO:0000313|EMBL:OJU54536.1};
OS Bacteroidales bacterium 45-6.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1895719 {ECO:0000313|EMBL:OJU54536.1, ECO:0000313|Proteomes:UP000185892};
RN [1] {ECO:0000313|EMBL:OJU54536.1, ECO:0000313|Proteomes:UP000185892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=45-6 {ECO:0000313|EMBL:OJU54536.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, 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:OJU54536.1}.
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DR EMBL; MKRS01000198; OJU54536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3M558; -.
DR Proteomes; UP000185892; Unassembled WGS sequence.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 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; IPR036291; NAD(P)-bd_dom_sf.
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 PRINTS; PR00082; GLFDHDRGNASE.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 53..181
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02812"
FT DOMAIN 198..309
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00208"
FT NON_TER 310
FT /evidence="ECO:0000313|EMBL:OJU54536.1"
SQ SEQUENCE 310 AA; 34138 MW; B87623D457852CC3 CRC64;
MKVENILATL EARHPGEAEY LQAVKEVLLS IEDVYNEHPE FEKAKLIERL VEPDRIFTFR
VSWVDDKGDV QVNIGYRVQF NNAIGPYKGG LRFHPSVNLS ILKFLGFEQT FKNALTTLPM
GGAKGGSDFN PKGKSNAEVM RFCQAFILEL WRNIGPDTDI PAGDIGVGGR EIGYLYGMYK
KLARENTGTF TGKGLDYGGS LIRPEATGFG GLYFVNEMLK NHGLDIQGKT IAISGFGNVA
WGAALKATEL GGKVVTISGP DGYIYDAEGI SGKKIDFLLE LRASGEDIVA PYADEFTNAK
FYEGKRPWEQ
//
