ID   DHE4_HALSI              Reviewed;         417 AA.
AC   Q5MBG2;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=NADP-specific glutamate dehydrogenase A1;
DE            EC=1.4.1.4;
GN   Name=gdhA1;
OS   Halobacterium salinarum (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=2242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-31.
RC   STRAIN=NRC-36014;
RX   PubMed=15780999; DOI=10.1016/j.gene.2005.01.011;
RA   Ingoldsby L.M., Geoghegan K.F., Hayden B.M., Engel P.C.;
RT   "The discovery of four distinct glutamate dehydrogenase genes in a strain
RT   of Halobacterium salinarum.";
RL   Gene 349:237-244(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-9, AND CATALYTIC ACTIVITY.
RC   STRAIN=NRC-36014;
RX   PubMed=12052548; DOI=10.1111/j.1574-6968.2002.tb11200.x;
RA   Hayden B.M., Bonete M.J., Brown P.E., Moir A.J., Engel P.C.;
RT   "Glutamate dehydrogenase of Halobacterium salinarum: evidence that the gene
RT   sequence currently assigned to the NADP+-dependent enzyme is in fact that
RT   of the NAD+-dependent glutamate dehydrogenase.";
RL   FEMS Microbiol. Lett. 211:37-41(2002).
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         Evidence={ECO:0000269|PubMed:12052548};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Strain NRC-36014 contains 4 distinct glutamate
CC       dehydrogenases while strain NRC-1 contains only 3.
CC       {ECO:0000305|PubMed:15780999}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; AY840085; AAW19065.1; -; Genomic_DNA.
DR   RefSeq; WP_012289198.1; NZ_CP038631.1.
DR   AlphaFoldDB; Q5MBG2; -.
DR   SMR; Q5MBG2; -.
DR   GeneID; 5953644; -.
DR   GeneID; 62886255; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12052548,
FT                   ECO:0000269|PubMed:15780999"
FT   CHAIN           2..417
FT                   /note="NADP-specific glutamate dehydrogenase A1"
FT                   /id="PRO_0000428789"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   CONFLICT        9
FT                   /note="S -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   417 AA;  45008 MW;  C18FA67CA33E81A1 CRC64;
     MPEANPFESL QEQLDDAGEF LDVNADVLER LKHPERVLET TLSVEMDDGT IETFKAFRSQ
     FNGDRGPYKG GIRYHPGVTR DEVKALSGWM VYKTAVADIP YGGGKGGIIL DPEEYSDSEL
     ERITRAFATE LRPFIGEDKD VPAPDVNTGQ REMNWIKDTY ETLEDTTAPG VITGKALENG
     GSEGRVNATG RSTMFAAREV FDYLDRDLSD ATVAVQGYGN AGSVAAKLIA DQGADVVAVS
     DSSGAVHNPD GLDTRAVKAF KTETGSVSGY EGATEELSNE ALLTMDVDLL VPAALENAID
     EDLAHDVDAD VVVEAANGPL TPDADDVLTE RGVTVVPDIL ANAGGVTVSY FEWVQNRQRF
     QWTEDRVNEE LEAIITDAFD AMTDAHEDAG TPNLRTAAYV VAVQRVVDAY EGSGSWP