ID Q2F5R4_BOMMO Unreviewed; 554 AA.
AC Q2F5R4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=glutamate dehydrogenase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00012889};
DE EC=1.4.1.3 {ECO:0000256|ARBA:ARBA00012889};
GN Name=692939 {ECO:0000313|EnsemblMetazoa:NP_001040245.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000313|EMBL:ABD36303.1};
RN [1] {ECO:0000313|EMBL:ABD36303.1}
RP NUCLEOTIDE SEQUENCE.
RA Niu B.L., Meng Z.Q., Weng H.B., Shen W.F., He L.H., Zheng K.F., Ye S.T.,
RA Lin T.B., Chen J.E.;
RT "Blast silkworm EST database for functional genes.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000313|Proteomes:UP000005204};
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [3] {ECO:0000313|EnsemblMetazoa:NP_001040245.1}
RP IDENTIFICATION.
RC STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:NP_001040245.1};
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
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=1.4.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023525};
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=1.4.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023549};
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ311359; ABD36303.1; -; mRNA.
DR RefSeq; NP_001040245.1; NM_001046780.1.
DR AlphaFoldDB; Q2F5R4; -.
DR SMR; Q2F5R4; -.
DR STRING; 7091.Q2F5R4; -.
DR PaxDb; 7091-BGIBMGA006507-TA; -.
DR EnsemblMetazoa; NM_001046780.1; NP_001040245.1; LOC692939.
DR GeneID; 692939; -.
DR KEGG; bmor:692939; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_025763_1_0_1; -.
DR InParanoid; Q2F5R4; -.
DR OMA; MIMGWMM; -.
DR OrthoDB; 45283at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR Gene3D; 1.10.287.140; -; 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; 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 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 2: Evidence at transcript level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Reference proteome {ECO:0000313|Proteomes:UP000005204}.
FT DOMAIN 261..551
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 554 AA; 61397 MW; 66511CD5CE8C6BE1 CRC64;
MLHLKNIAKS VVPPLKNSVQ NEALNTMFRI IPAGVNVCCR TYASHEIPDK LKDIPTSANP
KFFHMVEYFF HRACQVVEDK LVEDLKSRTP IEEKKKKVAG ILKLMEPCDH ILEIQFPLRR
DSGDYEMILG YRAQHSTHRT PTKGGIRFST DVTRDEVKAL SALMTFKCAC VDVPFGGAKA
GIKINPKEYS EHELEKITRR FTLELAKKGF IGPGVDVPAP DMGTGEREMS WIADTYAKTV
GFQDINAHAC VTGKPINQGG IHGRVSATGR GVFHGLENFI NEANYMSMIG TTPGWGGKTF
IVQGFGNVGL HTCRYLVRAG ATCIGVIEHD GSIYNPDGIN PKALEDYRIE NGTVVGFPGA
KAYEGENMLY EKCDILVPAA IEQVINKDNA HRIQAKIIAE AANGPTTPAA DKILIDRNIL
VIPDLYINAG GVTVSFFEWL KNLNHVSYGR LTFKYERESN YHLLESVQES LERRFGRVGG
RIPVTPSESF QKRISGASEK DIVHSGLDYT MERSARAIMK TAMRFNLGLD LRTAAYANSI
EKIFTTYADA GLAF
//
