DHE4_SALTY
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 03-AUG-2022, entry version 128.
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; Proteobacteria; 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; P15111; -.
DR PRIDE; P15111; -.
DR EnsemblBacteria; AAL20224; AAL20224; STM1299.
DR GeneID; 1252817; -.
DR KEGG; stm:STM1299; -.
DR PATRIC; fig|99287.12.peg.1380; -.
DR HOGENOM; CLU_025763_2_1_6; -.
DR OMA; HEPEFIQ; -.
DR PhylomeDB; P15111; -.
DR BioCyc; SENT99287:STM1299-MON; -.
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 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; 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
