ID E9FY41_DAPPU Unreviewed; 560 AA.
AC E9FY41;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=glutamate dehydrogenase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00012889};
DE EC=1.4.1.3 {ECO:0000256|ARBA:ARBA00012889};
GN ORFNames=DAPPUDRAFT_187316 {ECO:0000313|EMBL:EFX87470.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX87470.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX87470.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
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}.
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DR EMBL; GL732527; EFX87470.1; -; Genomic_DNA.
DR AlphaFoldDB; E9FY41; -.
DR STRING; 6669.E9FY41; -.
DR EnsemblMetazoa; EFX87470; EFX87470; DAPPUDRAFT_187316.
DR EnsemblMetazoa; XM_046606929.1; XP_046462885.1; LOC124209060.
DR KEGG; dpx:DAPPUDRAFT_187316; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_025763_1_0_1; -.
DR InParanoid; E9FY41; -.
DR OMA; MIMGWMM; -.
DR OrthoDB; 45283at2759; -.
DR PhylomeDB; E9FY41; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305}.
FT DOMAIN 257..556
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 560 AA; 62061 MW; 49AABBF6B0C57AED CRC64;
MLRFTAALLR NASSASTQNL LKLSPAAVQQ QTRLNSDIAY VIPEHLNGIE EAEDPLFFDM
VEFFYHKSCK ILQEKLVEDW RAPRMSTEEK RKKVKGLLNI IQPCHHVLEV SFPLKRDNGD
YEMITGYRAQ HSQHRLPCKG GIRYSDEVNI DEVKALSALM TFKCACVDVP FGGAKAGVKI
NPRKYSDNEL EKITRRFTLE LAKKGFIGPG IDVPAPDMGT GEREMAWIAD TYASTIGYND
INSHACVTGK PINQGGIHGR VSATGRGVFH GLENFLNEAS YMSMIGTTPG MGGKSVIIQG
FGNVGLHTAR YLHRAGATVI GIMEYDGSIV NPTGIDPKEL EDYKLQHGTI VGFPGAQPYT
GECLLYENCD ILVPAAIEKV INKHNAHRIQ AKIIAEAANG PTTPAADKIL IERNILVIPD
LYINAGGVTV SYFEWLKNLN HVSYGRLTFK YERESNHHLL ESIEQSLNTE SVQQSLERRF
GRVGGAIPIT PSESFQKRIS GASEKDIVHS GLDYSMERSA KAIMRTAMKY NLGIDLRSAA
YVNSVEKIFQ TYREAGLTFT
//
