ID DHE3_CHICK Reviewed; 503 AA. AC P00368; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 24-JAN-2024, entry version 127. DE RecName: Full=Glutamate dehydrogenase 1, mitochondrial; DE Short=GDH 1; DE EC=1.4.1.3 {ECO:0000250|UniProtKB:P00367}; DE Flags: Fragment; GN Name=GLUD1; Synonyms=GLUD; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=4735574; DOI=10.1016/s0021-9258(19)44013-1; RA Moon K., Piszkiewicz D., Smith E.L.; RT "Amino acd sequence of chicken liver glutamate dehydrogenase."; RL J. Biol. Chem. 248:3093-3107(1973). CC -!- FUNCTION: Mitochondrial glutamate dehydrogenase that converts L- CC glutamate into alpha-ketoglutarate. Plays a key role in glutamine CC anaplerosis by producing alpha-ketoglutarate, an important intermediate CC in the tricarboxylic acid cycle. {ECO:0000250|UniProtKB:P00367}. 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:0000250|UniProtKB:P00367}; 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:0000250|UniProtKB:P00367}; CC -!- ACTIVITY REGULATION: Subject to allosteric regulation. Activated by CC ADP. Inhibited by GTP and ATP. {ECO:0000250, CC ECO:0000250|UniProtKB:P00367}. CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P00366}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P00367}. CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P00367}. CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. CC {ECO:0000305}. 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 PIR; A00380; DECHE. DR STRING; 9031.ENSGALP00000043514; -. DR PaxDb; 9031-ENSGALP00000003139; -. DR VEuPathDB; HostDB:geneid_423612; -. DR eggNOG; KOG2250; Eukaryota. DR InParanoid; P00368; -. DR PhylomeDB; P00368; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central. DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA. DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; ISS:UniProtKB. DR GO; GO:0072350; P:tricarboxylic acid metabolic process; ISS:UniProtKB. 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; 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 1: Evidence at protein level; KW ATP-binding; Direct protein sequencing; Endoplasmic reticulum; GTP-binding; KW Mitochondrion; NADP; Nucleotide-binding; Oxidoreductase; KW Reference proteome. FT CHAIN <1..503 FT /note="Glutamate dehydrogenase 1, mitochondrial" FT /id="PRO_0000182742" FT ACT_SITE 129 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011" FT BINDING 87..89 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 93 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 117 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 122 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 198 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 212 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 216 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 265 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 268 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 384 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 389 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 395 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00366" FT BINDING 461 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00366" FT NON_TER 1 SQ SEQUENCE 503 AA; 55712 MW; 340DDB45BB0A5B04 CRC64; CZAADKEDDP NFFKMVEGFF DRGASIVEDK LVEGLRTRQS MEQRRHRVRG ILRIIKPCNH VLSVSFPIKR DDGZWEVIEG YRAQHSHQRT PCKGGIRYSL DVSVDEVKAL ASLMTYKCAV VDVPFGGAKA GVKINPKNYT DEDLEKITRR FTMELAKKGF IGPGVDVPAP NMSTGEREMS WIADTYASTI GHYDINAHAC VTKPGISQGG IHGRISATGR GLFGHIENFI ENASYMSILG MTPGFGDKTF AVQGFGNVGL HSMRYLHRFG AKCVAVGEFD GSIWNPDGID PKELEDYKLQ HGTIMGFPKA QKLEGSILET DCDILIPAAS EKQLTKANAH KVKAKIIAEG ANGPTTPQAD KIFLERNIMV IPDLYLNAGG VTVSAFZZKN LNHVSYGRLT FKYERDSNYH LLMSVQESLE RKFGKHGGTI PVVPTAEFQD RISGASEKDI VHSGLAYTME RSARQIMRTA MKYNLGLDLR TAAYVNAIEK VFKVYNEAGL TFT //