ID   A0A0P8ASB6_9SPHN        Unreviewed;       124 AA.
AC   A0A0P8ASB6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Glutamate dehydrogenase (NADP) {ECO:0000313|EMBL:KPQ22861.1};
DE            EC=1.4.1.4 {ECO:0000313|EMBL:KPQ22861.1};
DE   Flags: Fragment;
GN   ORFNames=HLUCCX21_05930 {ECO:0000313|EMBL:KPQ22861.1};
OS   Porphyrobacter sp. HL-46.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX   NCBI_TaxID=1479239 {ECO:0000313|EMBL:KPQ22861.1, ECO:0000313|Proteomes:UP000054043};
RN   [1] {ECO:0000313|EMBL:KPQ22861.1, ECO:0000313|Proteomes:UP000054043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-46 {ECO:0000313|EMBL:KPQ22861.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382}.
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:KPQ22861.1}.
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; LLEX01000259; KPQ22861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P8ASB6; -.
DR   STRING; 1479239.GCA_000744895_02172; -.
DR   eggNOG; COG0334; Bacteria.
DR   Proteomes; UP000054043; Unassembled WGS sequence.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   PANTHER; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KPQ22861.1}.
FT   DOMAIN          59..124
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02812"
FT   NON_TER         124
FT                   /evidence="ECO:0000313|EMBL:KPQ22861.1"
SQ   SEQUENCE   124 AA;  14490 MW;  AF775D5F463E87FE CRC64;
     MAVTDHVDLN QFMEGVKKRN PYQPEFVQAV QEVAEDIFEF MEDKEEYHSQ QILRRIAEPD
     RVVSFRVCWE DDNGNIRVQR GWRVQNNNAI GPYKGGIRFH PSVTESVLKF LAFEQTFKNA
     LTGL
//