ID DHE3_CHAAC Reviewed; 504 AA. AC P82264; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=Glutamate dehydrogenase, mitochondrial; DE Short=GDH; DE EC=1.4.1.3; GN Name=glud1; Synonyms=glud; OS Chaenocephalus aceratus (Blackfin icefish) (Chaenichthys aceratus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Notothenioidei; Channichthyidae; Chaenocephalus. OX NCBI_TaxID=36190; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=11087937; DOI=10.1016/s0167-4838(00)00186-2; RA Ciardiello M.A., Camardella L., Carratore V., di Prisco G.; RT "L-glutamate dehydrogenase from the antarctic fish Chaenocephalus aceratus. RT Primary structure, function and thermodynamic characterisation: RT relationship with cold adaptation."; RL Biochim. Biophys. Acta 1543:11-23(2000). 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 (By similarity). {ECO:0000250}. 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 -!- 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 -!- ACTIVITY REGULATION: Subject to allosteric regulation. Activated by CC ADP. Inhibited by GTP and ATP (By similarity). {ECO:0000250}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.0.; CC Temperature dependence: CC Optimum temperature is 30 degrees Celsius.; CC -!- SUBUNIT: Homohexamer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- MISCELLANEOUS: ADP can occupy the NADH binding site and activate the CC enzyme. {ECO:0000250}. 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 AlphaFoldDB; P82264; -. DR SMR; P82264; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:RHEA. 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: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; 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:SF33; GLUTAMATE DEHYDROGENASE [NAD(P)(+)]; 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. PE 1: Evidence at protein level; KW ATP-binding; Direct protein sequencing; GTP-binding; Mitochondrion; NAD; KW Nucleotide-binding; Oxidoreductase. FT CHAIN 1..504 FT /note="Glutamate dehydrogenase, mitochondrial" FT /id="PRO_0000182743" FT ACT_SITE 129 FT /evidence="ECO:0000250" 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" FT BINDING 117 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 122 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 198 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 212 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 216 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 265 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 268 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 384 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 390 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 396 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250" FT BINDING 462 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250" SQ SEQUENCE 504 AA; 55394 MW; D8E20681642E3E89 CRC64; ADAADKPDDP NFFRMVEGFF DRGASIVEDK LVEDLRTKET PEQKKGRVAG ILRIIKPCNH VLSLSFPIKR DNGEWEVIEG YRAQHSQHRT PCKGGIRYSM DVSVDEVKAL ASLMTYKCAV VDVPFGGAKA GVRINTKNYS DNELEKITRR FTIELAKKGF IGPGIDVPAP DMSTGEREMS WIADTYANTI AHTDINAHAC VTGKPISQGG IHGRISATGR GVFHGIENFM NEASYMSMVG LTPGVQDKTF VIQGFGNVGL HSMRYLHRFG AKCVGIGEID GAIYNADGID PKALEEYKLQ NGTIVGFPGA KPYEGSILEA DCDILIPAAG EKQLTRNNAR RIKAKIIAEG ANGPTTPDAD KIFLENNVMV IPDMYLNAGG VTVSYFEWLK NLNHVSYGRL TFKYERDSNY HLLMSVQESL ERKFGKQGGP IPVVPTADFQ ARVAGASEKD IVHSGLAYTM ERSARQIMRT ASKHNLGLDI RTAAYVNAIE KVFKVYNEAG LTFT //