ID A0A0G2APT3_9BACT Unreviewed; 328 AA.
AC A0A0G2APT3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KKW34754.1};
GN ORFNames=UY82_C0060G0002 {ECO:0000313|EMBL:KKW34754.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWC2_53_7.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618986 {ECO:0000313|EMBL:KKW34754.1, ECO:0000313|Proteomes:UP000033865};
RN [1] {ECO:0000313|EMBL:KKW34754.1, ECO:0000313|Proteomes:UP000033865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKW34754.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCRN01000060; KKW34754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2APT3; -.
DR PATRIC; fig|1618986.3.peg.638; -.
DR Proteomes; UP000033865; 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; 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; 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 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 180..326
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 328 AA; 35034 MW; 5B4642D9EF68B1CA CRC64;
MVNAFQTALA QLERAAQLKK IDSKIFERLR HLDREVVISI PVTMDDGMQK IFTGYRVEHN
NARGPYKGGI RYHQDVDINE VRALALWMTM KCAVAGIPMG GGKGGVTVNP KDLSEGELER
LTRGWAKGMM DILGPRKDVP APDVNTRSVE MDLIADEYAK ATGDASGAVI TGKSLEHGGS
EGRGTATAQG SFYVFEALRE KIGLPEKCRV VIQGFGNAGL HAAEIWTRAG HVLVATSDSK
GAVYKEDGLD VAALSAHKKT TGSVVNILGA ATITNAELLT TECDLLIPAA LENQITSANA
ADIKAKVVFE LANGPFSSCP TFLPTRVA
//
