ID   DHE4_SCHPO              Reviewed;         451 AA.
AC   P78804;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1999, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4;
DE   AltName: Full=NADP-dependent glutamate dehydrogenase;
GN   Name=gdh1; ORFNames=SPCC622.12c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-447.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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; CU329672; CAA21868.1; -; Genomic_DNA.
DR   EMBL; D89153; BAA13815.1; -; mRNA.
DR   PIR; T41492; T41492.
DR   RefSeq; NP_588184.1; NM_001023174.2.
DR   AlphaFoldDB; P78804; -.
DR   SMR; P78804; -.
DR   BioGRID; 275719; 47.
DR   STRING; 4896.SPCC622.12c.1; -.
DR   iPTMnet; P78804; -.
DR   MaxQB; P78804; -.
DR   PaxDb; P78804; -.
DR   PRIDE; P78804; -.
DR   EnsemblFungi; SPCC622.12c.1; SPCC622.12c.1:pep; SPCC622.12c.
DR   GeneID; 2539147; -.
DR   KEGG; spo:SPCC622.12c; -.
DR   PomBase; SPCC622.12c; gdh1.
DR   VEuPathDB; FungiDB:SPCC622.12c; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   HOGENOM; CLU_025763_2_1_1; -.
DR   InParanoid; P78804; -.
DR   OMA; HEPEFIQ; -.
DR   PhylomeDB; P78804; -.
DR   PRO; PR:P78804; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; ISO:PomBase.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IDA:PomBase.
DR   GO; GO:0019676; P:ammonia assimilation cycle; IDA:PomBase.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0097054; P:L-glutamate biosynthetic process; EXP:PomBase.
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   1: Evidence at protein level;
KW   NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..451
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182794"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   451 AA;  48790 MW;  DC05673E6A3433F5 CRC64;
     MSTPYEPEFQ QAYKEIVGSI ESSKLFEVHP ELKRVLPIIS IPERVLEFRV TWEDDKGNCR
     VNTGYRVQFN SALGPYKGGL RFHPSVNLSI LKFLGFEQIF KNALTGLPMG GGKGGSDFDP
     KGKSDNEIRR FSQAFMRQLF RYIGPQTDVP AGDIGVTGFV VMHMFGEYKR LRNEYSGVVT
     GKHMLTGGSN IRPEATGYGV VYYVKHMIEH RTKGAETLKG KRVAISGSGN VAQYAALKCI
     QEGAIVKSIS DSKGVLIAKT AEGLVPEEIH EIMALKEKRA SIADSASLCK KHHYIAGARP
     WTNVGEIDIA LPCATQNEVS GEEAAALIKQ GCRYVAEGSN MGSSAEAVEV FEKSRASGEG
     CWLAPGKAAN AGGVAVSGLE MAQNAQFSTW THAEVDAKLA GIMQNIFEQS TDVASKYCDS
     GSNNIPSLVD GANIAGFLKV ATAMQAVGDW W