ID A0A063XYR2_9GAMM Unreviewed; 450 AA.
AC A0A063XYR2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=ADINL_3094 {ECO:0000313|EMBL:KDE38639.1};
OS Nitrincola lacisaponensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE38639.1, ECO:0000313|Proteomes:UP000027318};
RN [1] {ECO:0000313|EMBL:KDE38639.1, ECO:0000313|Proteomes:UP000027318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4CA {ECO:0000313|EMBL:KDE38639.1,
RC ECO:0000313|Proteomes:UP000027318};
RX PubMed=16280482; DOI=10.1099/ijs.0.63647-0;
RA Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A.,
RA Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.;
RT "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic
RT bacterium isolated from an alkaline, saline lake.";
RL Int. J. Syst. Evol. Microbiol. 55:2273-2278(2005).
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC to alpha-ketoglutarate and ammonia. {ECO:0000256|ARBA:ARBA00003868}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001463};
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:KDE38639.1}.
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DR EMBL; JMSZ01000042; KDE38639.1; -; Genomic_DNA.
DR RefSeq; WP_036550072.1; NZ_JMSZ01000042.1.
DR AlphaFoldDB; A0A063XYR2; -.
DR STRING; 267850.ADINL_3094; -.
DR PATRIC; fig|267850.7.peg.3045; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000027318; Unassembled WGS sequence.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
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:UP000027318}.
FT DOMAIN 201..448
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 382
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 450 AA; 49474 MW; 392117519448814F CRC64;
MPYVHDTLLR LQKSSPAQTE FYQAAEEVLD SIRPLLDKDK HYREQGIIER LVEPERQIFF
RVVWHDDQGR VQVNKGYRVQ FNSALGPYKG GLRFHHSVNA GIIKFLGFEQ IFKNALTGLA
IGGGKGGSDF NPKGRSDMEV MRFCQAYMTE LHRHIGATMD VPAGDIGVGA REIGYLYGQY
KRLTGSYEGV LTGKGLNWGG SLARKEATGY GAVYFAENML QDRNDSLKNK VCLVSGAGNV
AIYTIEKLYE LGALPVTCSD SQGTLYHEQG IDLALLKDIK ERRRGALTEY LDSHPDARFI
SVDEYPADGH AVWRFKAQAA FPSATQNELT EADAQALLAN GVTCISEGAN MPSTAKAVDL
FLEAGICYGP GKAANAGGVA TSQLEMAQNA SMTQWSFEEV DNRLKEIMRG IYQRSSDTAR
EFNQPSNLVL GANIAGFRKV ADAMIDQGLV
//
