ID C0HA51_SALSA Unreviewed; 544 AA.
AC C0HA51;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Glutamate dehydrogenase 1, mitochondrial {ECO:0000256|ARBA:ARBA00040147};
DE EC=1.4.1.3 {ECO:0000256|ARBA:ARBA00012889};
GN Name=DHE3 {ECO:0000313|EMBL:ACN10920.1};
GN Synonyms=LOC106599099 {ECO:0000313|RefSeq:XP_014045638.1},
GN LOC106606089 {ECO:0000313|RefSeq:XP_014057685.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACN10920.1};
RN [1] {ECO:0000313|EMBL:ACN10920.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACN10920.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACN10920.1, ECO:0000313|RefSeq:XP_014045638.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACN10920.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACN10920.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACN10920.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:XP_014045638.1, ECO:0000313|RefSeq:XP_014057685.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014057685.1};
RG RefSeq;
RL Submitted (NOV-2023) 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}.
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DR EMBL; BT059207; ACN10920.1; -; mRNA.
DR RefSeq; XP_014045638.1; XM_014190163.1.
DR RefSeq; XP_014057685.1; XM_014202210.1.
DR STRING; 8030.ENSSSAP00000078003; -.
DR PaxDb; 8030-ENSSSAP00000078003; -.
DR GeneID; 106606089; -.
DR KEGG; sasa:106599099; -.
DR KEGG; sasa:106606089; -.
DR OrthoDB; 45283at2759; -.
DR Proteomes; UP000087266; Unplaced.
DR Bgee; ENSSSAG00000066078; Expressed in ovary and 15 other cell types or tissues.
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; 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.
PE 2: Evidence at transcript level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 251..540
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 544 AA; 60137 MW; 9CEFE61A64BEB86C CRC64;
MYRYFGELLT RGASSALASG CVKSALPVSA SLMRMRHYSE VAGEKDVDDP NFFGMVEGFF
DRGANIVEDK LVEDLKNKET PVQKRHRVRG ILKIIKPCNH ILSVSFPIKR DNGEWEVIEG
YRAQHSQHRT PCKGGIRYST EVSVDEVKAL ASLMTYKCAV VDVPFGGAKA GVKINVKNYT
DNELEKITRR FTIELAKKGF IGPGIDVPAP DMSTGEREMS WIADTYANTM GHHDINAHAC
VTGKPISQGG IHGRISATGR GVFHGIENFV NETAYMSQLG LSPGFTDKTF VIQGFGNVGM
HSMRYLHRFG AKCVGVGEMD GSIWNPSGID PKELEDYKLQ HGTIVGFPNS TPYKGSILEA
DCDILIPAAS EKQLTRNNAH KIKAKIIAEG ANGPTTPDAD KIFLERNIMV IPDMYLNAGG
VTVSYFEWLK NLNHVSYGRL TFKYERDSNY HLLMSVQESL ERKFGKHGGA IPVVPTSEFQ
ARIAGASEKD IVHSGLAYTM ERSARQIMRT ANKYNLGLDL RTAAYVNAIE KVFKVYNEAG
VTFT
//
