DHE3_CHICK
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 03-AUG-2022, entry version 122.
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}.
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DR PIR; A00380; DECHE.
DR STRING; 9031.ENSGALP00000003139; -.
DR PaxDb; P00368; -.
DR VEuPathDB; HostDB:geneid_423612; -.
DR eggNOG; KOG2250; Eukaryota.
DR InParanoid; P00368; -.
DR PhylomeDB; P00368; -.
DR Proteomes; UP000000539; Unplaced.
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 InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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.
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
