ID I3YVE3_AEQSU Unreviewed; 431 AA.
AC I3YVE3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=Aeqsu_1470 {ECO:0000313|EMBL:AFL80961.1};
OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL80961.1, ECO:0000313|Proteomes:UP000006049};
RN [1] {ECO:0000313|EMBL:AFL80961.1, ECO:0000313|Proteomes:UP000006049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC {ECO:0000313|Proteomes:UP000006049};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Aequorivita sublithincola DSM 14238.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP003280; AFL80961.1; -; Genomic_DNA.
DR RefSeq; WP_014782218.1; NC_018013.1.
DR AlphaFoldDB; I3YVE3; -.
DR STRING; 746697.Aeqsu_1470; -.
DR KEGG; asl:Aeqsu_1470; -.
DR PATRIC; fig|746697.3.peg.1492; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_1_2_10; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000006049; Chromosome.
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; cd01076; NAD_bind_1_Glu_DH; 1.
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}.
FT DOMAIN 197..428
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 156
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 431 AA; 47618 MW; 61DF88602A870CC0 CRC64;
MTNEQTVEKP KPLKRGMLDN VLEQFNSAAD KIDLNPNVRK ILSITNTEII IHFPVRMDNG
EVEVFTGYRV QHNNALGPYK GGLRYHPTVD IDAARALAMW MTWKTSLAGL PYGGAKGGIQ
IDPSIYSKGE LERITRRFTY ALGENIGPEH DIPAPDVNTN DQTMAWIADT YMSTKSTSER
SKNQHVVTGK PVGSGGLEGR DRATGYGVYL TIKFWSEKNN ETLKGKKFIV QGFGNVGYWA
AHFLENEGAL LVGVQDAFGS VQNQKGITVE DLFNYGKANN GSIVGFPEAS AMEGKDFFAL
DCDICIPAAL GNQITKDNAR SIKASLIAEG ANGPTDVEGE KILIERGITI IPDIMCNSGG
VIGSYFEWLQ NRNGELWQMD EILEKLEKKL RTTFKKVTAY SEENNIDMRT AAFSIAIARI
EKAYILRGIF P
//
