ID   DHE4_SALTY              Reviewed;         447 AA.
AC   P15111;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4;
GN   Name=gdhA; OrderedLocusNames=STM1299;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2656714; DOI=10.1016/s0021-9258(18)81733-1;
RA   Bansal A., Dayton M.A., Zalkin H., Colman R.F.;
RT   "Affinity labeling of a glutamyl peptide in the coenzyme binding site of
RT   NADP+-specific glutamate dehydrogenase of Salmonella typhimurium by 2-[(4-
RT   bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 2',5'-bisphosphate.";
RL   J. Biol. Chem. 264:9827-9835(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; M24021; AAA27131.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20224.1; -; Genomic_DNA.
DR   PIR; A33504; A33504.
DR   RefSeq; NP_460265.1; NC_003197.2.
DR   RefSeq; WP_000372869.1; NC_003197.2.
DR   AlphaFoldDB; P15111; -.
DR   SMR; P15111; -.
DR   STRING; 99287.STM1299; -.
DR   PaxDb; 99287-STM1299; -.
DR   GeneID; 1252817; -.
DR   KEGG; stm:STM1299; -.
DR   PATRIC; fig|99287.12.peg.1380; -.
DR   HOGENOM; CLU_025763_2_1_6; -.
DR   OMA; PCFAAFP; -.
DR   PhylomeDB; P15111; -.
DR   BioCyc; SENT99287:STM1299-MONOMER; -.
DR   SABIO-RK; P15111; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
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; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 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   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..447
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182776"
FT   ACT_SITE        128
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            168
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        299
FT                   /note="E -> D (in Ref. 1; AAA27131)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  48574 MW;  CB94B38B5042E0A2 CRC64;
     MDQTCSLESF LNHVQKRDPH QTEFAQAVRE VMTTLWPFLE QNPRYRHMSL LERLVEPERV
     IQFRVVWLDD KNQVQVNRAW RVQFNSAIGP YKGGMRFHPS VNLSILKFLG FEQTFKNALT
     TLPMGGGKGG SDFDPKGKSE GEVMRFCQAL MTELYRHLGP DTDVPAGDIG VGGREVGFMA
     GMMRKLSNNS SCVFTGKGLS FGGSLIRPEA TGYGLVYFTE AMLKRHGLGF EGMRVAVSGS
     GNVAQYAIEK AMAFGARVVT ASDSSGTVVD ESGFTPEKLA RLCEIKASRD GRVADYAREF
     GLTYLEGQQP WSVPVDIALP CATQNELDVD AARVLIANGV KAVAEGANMP TTIEATDLFL
     EAGVLFAPGK AANAGGVATS GLEMAQNAAR LSWKAEKVDA RLHHIMLDIH HACVEYGGDN
     KHTNYVQGAN IAGFVKVADA MLAQGVI
//