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Database: UniProt
Entry: V8G8D4_9BURK
LinkDB: V8G8D4_9BURK
Original site: V8G8D4_9BURK 
ID   V8G8D4_9BURK            Unreviewed;       451 AA.
AC   V8G8D4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=V757_05540 {ECO:0000313|EMBL:ETD72213.1};
OS   Pelistega indica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pelistega.
OX   NCBI_TaxID=1414851 {ECO:0000313|EMBL:ETD72213.1, ECO:0000313|Proteomes:UP000018766};
RN   [1] {ECO:0000313|EMBL:ETD72213.1, ECO:0000313|Proteomes:UP000018766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM-7 {ECO:0000313|EMBL:ETD72213.1,
RC   ECO:0000313|Proteomes:UP000018766};
RA   Kumbhare S.V., Shetty S.A., Sharma O., Dhotre D.P.;
RT   "Genomic analysis of Pelistega sp. HM-7.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
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:ETD72213.1}.
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DR   EMBL; AYSV01000072; ETD72213.1; -; Genomic_DNA.
DR   RefSeq; WP_023950584.1; NZ_CABMIG010000072.1.
DR   AlphaFoldDB; V8G8D4; -.
DR   PATRIC; fig|1414851.3.peg.1121; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000018766; Unassembled WGS sequence.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 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; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 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:UP000018766}.
FT   DOMAIN          201..449
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        125
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         208
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         239
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            165
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   451 AA;  49416 MW;  7279EC0031C7355F CRC64;
     MSLIKDTLSR IQQSSPGEPE FYQAVEEVLE SLEPLFKKEK KYSEHNIIQR IVEPERMITF
     RVTWIDDKGK IQVNKGYRVQ FSSAIGPYKG GLRFHPSVNS GIIKFLGFEQ IFKNSLTGLP
     IGGGKGGSDF DPKGKSDNEI MRFCQSFMTE LYRHIGDTID IPAGDIGVGG REIGYLYGQY
     KRLTGSYEGV LTGKKIPWGG SLARTEATGY GAVYFADSLL TSRNDQLAGK TAVVSGSGNV
     AIYTIKKLIE MGATPVSCSD SRGFIYHKTG INLNTLQQLK EQGKNESLEE YAKIHKDAKY
     TPVKDYPKGR NPVWSIKCDL AFPSATQNEL NLADAKELLK NGCILVAEGA NMPSTPEAVH
     AFLEAKILYG PGKAANAGGV ATSQLEMSQN ASMLQWSFEE VDGRLRNIMH NIYLSASQTA
     EEFGQPHNLV LGANIAGFRK VANAMIDQGA V
//
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