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Database: UniProt
Entry: A0A0C2E8A6_9STAP
LinkDB: A0A0C2E8A6_9STAP
Original site: A0A0C2E8A6_9STAP 
ID   A0A0C2E8A6_9STAP        Unreviewed;       414 AA.
AC   A0A0C2E8A6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=SN16_02465 {ECO:0000313|EMBL:KIH71557.1};
OS   Salinicoccus roseus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX   NCBI_TaxID=45670 {ECO:0000313|EMBL:KIH71557.1, ECO:0000313|Proteomes:UP000031546};
RN   [1] {ECO:0000313|EMBL:KIH71557.1, ECO:0000313|Proteomes:UP000031546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W12 {ECO:0000313|EMBL:KIH71557.1,
RC   ECO:0000313|Proteomes:UP000031546};
RA   Wang H., Yu B.;
RT   "Genome sequences of high lactate-tolerant strain Salinicoccus roseus W12
RT   with industrial interest.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC         NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000477};
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC       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:KIH71557.1}.
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DR   EMBL; JXII01000002; KIH71557.1; -; Genomic_DNA.
DR   RefSeq; WP_040105021.1; NZ_JXII01000002.1.
DR   AlphaFoldDB; A0A0C2E8A6; -.
DR   STRING; 45670.SN16_02465; -.
DR   GeneID; 77844402; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000031546; Unassembled WGS sequence.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR   Gene3D; 1.10.8.1210; -; 2.
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; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
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   PIRSF; PIRSF000185; Glu_DH; 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   NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031546}.
FT   DOMAIN          183..412
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         221
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            146
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   414 AA;  45516 MW;  CDF3A7A7BAC663E6 CRC64;
     MGEKSNLITS TQKIIHQALD NLGYDEGMYE LIKEPLRVLK VRIPVEMDDG STKVFTGYRA
     QHNDAAGPTK GGIRFHPDVT EDEVVALSMW MTLKAGIVDI PYGGGKGGVI CDPRVMSTRE
     LEGVARGYVR AVSQIVGPTK DIPAPDVYTN AQVMAWMMDE YSVKNSDDPF QFITGKPISV
     GGSKGRETAT AMGAVICVEQ AMEKRGIPIE EARVVVQGFG NAGSYISKML YDKGAKIVGI
     SRSSRALYNP EGIDIDYVLD NREKVDLADH MAVSVLSNEE LLELDCDVLI PAAIANQVTE
     LNAERIKADI ICEAANGPTT EEATRILTEK GALIIPDVLA SAGGVTVSYF EWVQNKQGFY
     WEEDEIQELL EKKMKSAFDT IYDLHEARNM DMRLAAYTVG IKRTSEAVRF RGWA
//
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