ID Q095H5_STIAD Unreviewed; 327 AA.
AC Q095H5;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Glutamate dehydrogenase B {ECO:0000313|EMBL:EAU67376.1};
DE EC=1.4.1.3 {ECO:0000313|EMBL:EAU67376.1};
GN ORFNames=STIAU_7917 {ECO:0000313|EMBL:EAU67376.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU67376.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU67376.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU67376.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) 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:EAU67376.1}.
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DR EMBL; AAMD01000034; EAU67376.1; -; Genomic_DNA.
DR AlphaFoldDB; Q095H5; -.
DR PATRIC; fig|378806.16.peg.6618; -.
DR Proteomes; UP000032702; 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 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF24; GLUTAMATE DEHYDROGENASE 2; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 96..326
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 327 AA; 35451 MW; 02FA5593B27100EE CRC64;
MASLMTWKTA VTNLPYGGAK GGITCDPSQL SLKELERLTR KYVDQVQDVI GPSRDIPAPD
VNTNPQVMAW IMDQYSRYHG HSPAVVTGKP LELYGSKGRE AATGRGLLYI CREILRDVNL
PMKGTRFAIQ GFGNVGSHVA RLLWEEGAVV VAVSDMLGGV RNPQGLDIAS LFEHVQRSGT
VTGYGGGTPC SHEEVLAADC EVLIPAALGH ALNRENANAV RARLIVEGAN GPTSPEADEL
LEKRGVLVVP DILANAGGVT VSYFEWVQNL QHLAWEEDRV NAELERTVKE SYERVTQIAR
SRKVSLRTAA FILAIGRVGK ATVMRGI
//
