ID   DHE4_HAEIN              Reviewed;         449 AA.
AC   P43793;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4;
GN   Name=gdhA; OrderedLocusNames=HI_0189;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC21858.1; -; Genomic_DNA.
DR   PIR; A64053; A64053.
DR   RefSeq; NP_438358.1; NC_000907.1.
DR   RefSeq; WP_005664327.1; NC_000907.1.
DR   AlphaFoldDB; P43793; -.
DR   SMR; P43793; -.
DR   STRING; 71421.HI_0189; -.
DR   PRIDE; P43793; -.
DR   EnsemblBacteria; AAC21858; AAC21858; HI_0189.
DR   KEGG; hin:HI_0189; -.
DR   PATRIC; fig|71421.8.peg.194; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_2_1_6; -.
DR   OMA; PCFAAFP; -.
DR   PhylomeDB; P43793; -.
DR   BioCyc; HINF71421:G1GJ1-200-MON; -.
DR   Proteomes; UP000000579; 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..449
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182770"
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"
SQ   SEQUENCE   449 AA;  48660 MW;  4698E0CD6C665A34 CRC64;
     MSKVASLDAF LTKVAQRDGY QPEFLQAVRE VFTSIWPFLE ANPKYRSEAL LERLVEPERA
     FQFRVAWTDD KGQVQVNRAF RVQFNSAIGP FKGGMRFHPS VNLSILKFLG FEQIFKNALT
     TLPMGGAKGG SDFDPKGKSD AEVMRFCQAL MAELYRHVGA DTDVPAGDIG VGGREVGYLA
     GYMKKLSNQS ACVFTGRGLS FGGSLIRPEA TGYGLIYFAQ AMLAEKGDSF AGKVVSVSGS
     GNVAQYAIEK ALSLGAKVVT CSDSSGYVYD PNGFTTEKLA ALFDIKNTKR GRVKDYAEQF
     GLQYFEGKRP WEVQVDIALP CATQNELELS DAQRLIKNGV KLVAEGANMP TTIEATEALL
     AADVLFGPGK AANAGGVATS GLEMAQSSQR LYWTAEEVDA QLHRIMLDIH ANCKKYGTIE
     GQENINYVVG ANVAGFVKVA DAMLAQGVY