ID   A8M7B0_SALAI            Unreviewed;       395 AA.
AC   A8M7B0;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Glutamate dehydrogenase (NAD(P)+) {ECO:0000313|EMBL:ABV98783.1};
GN   OrderedLocusNames=Sare_2957 {ECO:0000313|EMBL:ABV98783.1};
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=391037 {ECO:0000313|EMBL:ABV98783.1};
RN   [1] {ECO:0000313|EMBL:ABV98783.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205 {ECO:0000313|EMBL:ABV98783.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382}.
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DR   EMBL; CP000850; ABV98783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8M7B0; -.
DR   STRING; 391037.Sare_2957; -.
DR   KEGG; saq:Sare_2957; -.
DR   PATRIC; fig|391037.6.peg.2991; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_7_0_11; -.
DR   OrthoDB; 9803297at2; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
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   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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          153..372
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   395 AA;  41552 MW;  C1C7FEDEA7C590D2 CRC64;
     MNTVIEYRDP IEGFSGWLVY DGLDCRLAAG GCRVAPGLTP SLLAELARRM RLKERLLGIN
     VDGAKCGIDY DPHAPGKAAA VRRFLAFLRP ELMRRYSMGC DMGTRWEELE SLARLEDIPS
     VKYAVRGAQE LTEDDFTARL ALLGQRVDDL TLGNRRAGHA LAQAALVAAD AAGLPGPLVG
     TLQGFGTLGR AAACTLARSG VRITAVADEY GCVASHDGLD VAGMLGGRPG TPVQQLAPDA
     VHLPSDSLFG LPTDLVLLAA GEDAVPVERA RRPQAPVVVV GANCGLSPES EQVLYDAGVL
     VVPDVVGGIG GSASMEALFG APSCPSPAGV LAGVTDLMWQ LVGHLVDESR RRKLPLRQVA
     YDVVSAAVVS PGDRPYGLSP YRTRALTVAS TLARR
//