ID   DHE4_PSYT1              Reviewed;         448 AA.
AC   Q9S1F9;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4 {ECO:0000269|PubMed:10601858};
GN   Name=gdhA; Synonyms=gdh {ECO:0000303|PubMed:10601858};
OS   Psychrobacter sp. (strain TAD1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=81861;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-448, FUNCTION AS A
RP   GLUTAMATE DEHYDROGENASE, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=TAD1;
RX   PubMed=10601858; DOI=10.1046/j.1432-1327.2000.00972.x;
RA   Di Fraia R., Wilquet V., Ciardiello M.A., Carratore V., Antignani A.,
RA   Camardella L., Glansdorff N., Di Prisco G.;
RT   "NADP+-dependent glutamate dehydrogenase in the Antarctic psychrotolerant
RT   bacterium Psychrobacter sp. TAD1. Characterization, protein and DNA
RT   sequence, and relationship to other glutamate dehydrogenases.";
RL   Eur. J. Biochem. 267:121-131(2000).
CC   -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC       to alpha-ketoglutarate and ammonia. {ECO:0000269|PubMed:10601858}.
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         Evidence={ECO:0000269|PubMed:10601858};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.043 mM for NADP (at 20 degrees Celsius and at pH 8)
CC         {ECO:0000269|PubMed:10601858};
CC         KM=4 mM for ammonium (at 20 degrees Celsius and at pH 8)
CC         {ECO:0000269|PubMed:10601858};
CC         KM=67.4 mM for L-glutamate (at 20 degrees Celsius and at pH 8)
CC         {ECO:0000269|PubMed:10601858};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:10601858};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.
CC         {ECO:0000269|PubMed:10601858};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:10601858}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; AJ010746; CAB54142.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S1F9; -.
DR   SMR; Q9S1F9; -.
DR   PRIDE; Q9S1F9; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IMP:UniProtKB.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IMP:UniProtKB.
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   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   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10601858"
FT   CHAIN           2..448
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182774"
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         375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            164
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   448 AA;  49448 MW;  EE24FEA463DCB660 CRC64;
     MSISKAIEKV EARYAHQPEF IQAVKEVAIT IKPLYDAHPE YDKLKVFERL VEPDRVFGFR
     VNWEDDNGEI QINRGWRVQF SNALGPYKGG LRFHPTVNQS VLKFLGFEQI FKNALTGLPI
     GGGKGGSDFD PKGKTDSEIR RFCYAFMREL HHYVNKDMDV PAGDIGVGGR EVSYMFAMYK
     NLTRESTGVI TGKGVGFGGS LMRTEATGYG AVYFLQNMLA AQNESIEGKK VLVSGAGNVS
     LHAAEKATLI GAIVLTVSDS KGTIYDAKGL NQEKIDWLKV QKDQHKPLAD YVEVFGGEWM
     ADQKPWSIKA DIAIPSATQN EINEEDAKLL VDNGVKYIVE GANMPLTAEA IDYIRLHRVH
     YAPGKAANAG GVAVSALEMS QNSVRQYQTF EQVDERLQGI MKDIHDSSAQ ASEMYGQTDE
     GYIDYMSGAN MVGFKRVADA LVAFGILN