ID   DHE4_UNKP               Reviewed;         446 AA.
AC   P14657;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4;
GN   Name=gdhA;
OS   Unknown prokaryotic organism.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=2725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2690019; DOI=10.1093/nar/17.24.10500;
RA   Cock J.M., Schmidt R.R.;
RT   "A glutamate dehydrogenase gene sequence.";
RL   Nucleic Acids Res. 17:10500-10500(1989).
CC   -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC       to a-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}.
CC   -!- CAUTION: This sequence originates from an organism contaminating a
CC       Chlorella sorokiniana culture, probably a bacterium. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X16399; CAA34434.1; -; Genomic_DNA.
DR   AlphaFoldDB; P14657; -.
DR   SMR; P14657; -.
DR   PRIDE; P14657; -.
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..446
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182778"
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         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            168
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   446 AA;  48490 MW;  EDCD53EF87F1A090 CRC64;
     MEYAVSVESF LSSLQRHNPH QPEYLQAVRE VFTSLWPFIE RNPAYREQAL LERLVEPERI
     IQFRVSWVDD RGQVQVNRAF RVQFNSAIGP YKGGMRFHPS VNLSILKFLG FEQTFKNALT
     TLPMGGGKGG SDFDPKGKSQ GRIMRFCQAL MTELYRHLGP DTDVPAGDIG DGGREVGFMA
     GMMKKLSNNT ACVFTGKGLS FGGSLIRPEA TGYGLVYFTD AMLQRHGLGF EGMRVAVSGS
     GNVAQYTIEK ALELDARVIT VSDSGGTLVD EDGFTTEKLA HLAEIKNQRY GRVADYAAER
     GLTYLAGQQP WNVPVDIALP CATQNELDLE AARVIRNGVK AVAEGANMPT TIQATDAFLD
     AGVLFAPGKA ANAAGLATSG LEMAQNAARI GWRAEKVDVR LQHIMADIHH ACVEYGGEGK
     QTHYVHGANI AGFVKVAEAM LAQGVL