DHE3_CHAAC
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 03-AUG-2022, entry version 92.
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}.
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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 InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 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
