ID   DHE4_HELPJ              Reviewed;         448 AA.
AC   Q9ZKD8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4;
GN   Name=gdhA; OrderedLocusNames=jhp_1001;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC       to alpha-ketoglutarate and ammonia. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; AE001439; AAD06574.1; -; Genomic_DNA.
DR   PIR; F71862; F71862.
DR   RefSeq; WP_000289195.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZKD8; -.
DR   SMR; Q9ZKD8; -.
DR   IntAct; Q9ZKD8; 1.
DR   STRING; 85963.jhp_1001; -.
DR   PRIDE; Q9ZKD8; -.
DR   EnsemblBacteria; AAD06574; AAD06574; jhp_1001.
DR   KEGG; hpj:jhp_1001; -.
DR   PATRIC; fig|85963.30.peg.1590; -.
DR   eggNOG; COG0334; Bacteria.
DR   OMA; PCFAAFP; -.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0006537; P:glutamate biosynthetic process; ISS:UniProtKB.
DR   CDD; cd05313; NAD_bind_2_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..448
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182772"
FT   ACT_SITE        124
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            164
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   448 AA;  49491 MW;  1E25BAC991C4FCCB CRC64;
     MYVEKILQSL QKKYPYQKEF HQAVYEAITS LKPLLDSDKS YEKHAVLERL IEPEREIFFR
     VCWLDDNHQI QVNRGCRVEF NSAIGPYKGG LRFHPSVNES VIKFLGFEQV LKNSLTTLAM
     GGAKGGSDFD PKEKSEHEIM RFCQAFMNEL YRHIGATTDV PAGDIGVGER EIGYLFGQYK
     KLVNRFEGVL TGKGLTYGGS LCRKEATGYG CVYFAEEMLQ ERNSSLEGKV CSVSGSGNVA
     IYTIEKLLQI GAKPVTASDS NGMIYDKDGI DLELLKEIKE ARRGRIKEYA LEKTSAKYTP
     TENYPKGGNA IWHVPCFAAF PSATENELSV LDAKTLLSNG CKCVAEGANM PSSNEAIELF
     LQAKISYGIG KAANAGGVSV SGLEMAQNAS MHPWSFEVVD AKLHHIMKEI YKNVSQTAKE
     FKDPTNFVLG ANIAGFRKVA SAMIAQGV