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Database: UniProt
Entry: DHE3_AERPE
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Original site: DHE3_AERPE 
ID   DHE3_AERPE              Reviewed;         418 AA.
AC   Q9YC65;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   28-JUN-2023, entry version 115.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
GN   Name=gdhA; OrderedLocusNames=APE_1386.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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:0000255|PROSITE-ProRule:PRU10011};
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:0000255|PROSITE-ProRule:PRU10011};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; BA000002; BAA80383.2; -; Genomic_DNA.
DR   PIR; A72616; A72616.
DR   AlphaFoldDB; Q9YC65; -.
DR   SMR; Q9YC65; -.
DR   STRING; 272557.APE_1386.1; -.
DR   EnsemblBacteria; BAA80383; BAA80383; APE_1386.1.
DR   KEGG; ape:APE_1386.1; -.
DR   eggNOG; arCOG01352; Archaea.
DR   BRENDA; 1.4.1.4; 171.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 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   3: Inferred from homology;
KW   Cytoplasm; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..418
FT                   /note="Glutamate dehydrogenase"
FT                   /id="PRO_0000182754"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         217..223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  46171 MW;  7C0A806BB62CA6E5 CRC64;
     MQPTDPLEEA RAQLRRAVDL LGYDDYVYEV LANPDRVLQV RVTIKMDDGT VKTFLGWRSQ
     HNSALGPYKG GVRYHPNVTM NEVIALSMWM TWKNSLAGLP YGGGKGGVRV NPKILSPREL
     ELLSRKYFES ISDIVGVDQD IPAPDVYTDP QVMSWFLDEY NRVKRGQFFG VVTGKPVELG
     GLNARIVSTG YGVAVSTRVA AEKFLGGLEG RTVAVQGYGN VGYYAAKFLA EMGAKIVAVS
     DSRGGIYDPE GIDPEEALKV KRSTGTVANY QRGKKISTME ILELPVDILV PAAIEEVITD
     ENADRIKAKI ISEGANGPTT TAAEKILVKK GVLVLPDILA NAGGVIMSHI EWVNNRMGGW
     ITDEEALKKL EQKMVENTKT VITYWEKNLK PEENSLRDAA YMIAVERVFR AMKLRGWI
//
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