ID A0A140T871_BOVIN Unreviewed; 561 AA.
AC A0A140T871;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Glutamate dehydrogenase 1, mitochondrial {ECO:0000256|ARBA:ARBA00040147};
DE EC=1.4.1.3 {ECO:0000256|ARBA:ARBA00012889};
GN Name=GLUD1 {ECO:0000313|Ensembl:ENSBTAP00000009923.4};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000009923.4, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000009923.4, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000009923.4,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ADP.
RX PubMed=36232607; DOI=10.3390/ijms231911306;
RA Aleshin V.A., Bunik V.I., Bruch E.M., Bellinzoni M.;
RT "Structural Basis for the Binding of Allosteric Activators Leucine and ADP
RT to Mammalian Glutamate Dehydrogenase.";
RL Int. J. Mol. Sci. 23:11306-11306(2022).
RN [3] {ECO:0000313|Ensembl:ENSBTAP00000009923.4}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000009923.4};
RG Ensembl;
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 RefSeq; NP_872593.2; NM_182652.2.
DR PDB; 8AR7; X-ray; 2.45 A; A/B/C/D/E/F=1-561.
DR PDB; 8AR8; X-ray; 2.40 A; A/B/C/D/E/F=1-561.
DR AlphaFoldDB; A0A140T871; -.
DR SMR; A0A140T871; -.
DR Ensembl; ENSBTAT00000009923.5; ENSBTAP00000009923.4; ENSBTAG00000007540.6.
DR GeneID; 281785; -.
DR KEGG; bta:281785; -.
DR CTD; 2746; -.
DR VEuPathDB; HostDB:ENSBTAG00000007540; -.
DR GeneTree; ENSGT00390000000854; -.
DR InParanoid; A0A140T871; -.
DR OMA; MIMGWMM; -.
DR OrthoDB; 45283at2759; -.
DR Reactome; R-BTA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-BTA-8964539; Glutamate and glutamine metabolism.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000007540; Expressed in temporal cortex and 104 other cell types or tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
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 GO; GO:0006541; P:glutamine metabolic process; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0072350; P:tricarboxylic acid metabolic process; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8};
KW Nucleotide-binding {ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A140T871};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 268..557
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT BINDING 145
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8"
FT BINDING 146
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8"
FT BINDING 179
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8"
FT BINDING 180
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8"
FT BINDING 269
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8"
FT BINDING 447
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8"
FT BINDING 453
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8"
FT BINDING 456
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8"
FT BINDING 519
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:8AR7, ECO:0007829|PDB:8AR8"
SQ SEQUENCE 561 AA; 61631 MW; EA81C62B0198521B CRC64;
MYRCLGEALL LSRIGPAALG SVAADSAVLL GRARGQAAAA VAAPQPGLVP PARRHYSEAA
ADREDDPNFF KMVEGFFDRG ASIVEDKLVE DLKTRETEEQ KRNRVRGILR IIKPCNHVLS
LSFPIRRDDG SWEVIEGYRA QHSQHRTPCK GGIRYSTDVS VDEVKALASL MTYKCAVVDV
PFGGAKAGVK INPKNYTDNE LEKITRRFTM ELAKKGFIGP GVDVPAPDMS TGEREMSWIA
DTYASTIGHY DINAHACVTG KPISQGGIHG RISATGRGVF HGIENFINEA SYMSILGMTP
GFGDKTFAVQ GFGNVGLHSM RYLHRFGAKC VAVGESDGSI WNPDGIDPKE LEDFKLQHGT
ILGFPKAKIY EGSILEVDCD ILIPAASEKQ LTKSNAPRVK AKIIAEGANG PTTPEADKIF
LERNIMVIPD LYLNAGGVTV SYFEWLKNLN HVSYGRLTFK YERDSNYHLL MSVQESLERK
FGKHGGTIPI VPTAEFQDRI SGASEKDIVH SGLAYTMERS ARQIMRTAMK YNLGLDLRTA
AYVNAIEKVF RVYNEAGVTF T
//
