ID   DHE4_SACSH              Reviewed;         390 AA.
AC   P39475;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4;
DE   Flags: Fragment;
GN   Name=gdhA;
OS   Saccharolobus shibatae (Sulfolobus shibatae).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=2286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8125334; DOI=10.1016/0378-1119(94)90725-0;
RA   Benachenhou-Lahfa N., Labedan B., Forterre P.;
RT   "PCR-mediated cloning and sequencing of the gene encoding glutamate
RT   dehydrogenase from the archaeon Sulfolobus shibatae: identification of
RT   putative amino-acid signatures for extremophilic adaptation.";
RL   Gene 140:17-24(1994).
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=1.4.1.4;
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; X73990; CAA52168.1; -; Genomic_DNA.
DR   PIR; S37407; S37407.
DR   AlphaFoldDB; P39475; -.
DR   SMR; P39475; -.
DR   PRIDE; P39475; -.
DR   BRENDA; 1.4.1.4; 6162.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   NADP; Oxidoreductase.
FT   CHAIN           <1..390
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182781"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   NON_TER         1
SQ   SEQUENCE   390 AA;  42091 MW;  BCB9ACFE6AC9CEB2 CRC64;
     LDTLEALSQP ERVIQVKIQI RGSDGKLKTF MGWRSQHNSA LGPYKGGVRY SPNVTQDEVI
     ALSMIMTWKN SLLLLPYGGG KGGIRVDPKK LTLKELEDLS RKYVQLIHNY LGSDVDIPAP
     DINTNPQTMA WFLDEYIKIT GEVDFAVFTG KPSELGGIGV RLYSTGLGVA TIAREAANKF
     IGGIEGSRVI IQGFGNVGSF TAKFLNEMGA KIIGVSDIGG GVISDDGIDV NKALEVVQST
     GSVVNYPEGK KVTNEELLTS DCDILIPAAV ENVINKFNAP KVKAKLIVEG ANGPLAADAD
     EIIKQRGIVV IPDILANAGG VVGSYVEWAN NKSGGIISDE EAKKLIIDRM TNAFNALYEF
     HKRKFADQDL RTVAMALRVD RVVGMKARAI