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   16-JUN-2009, entry version 54.
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 (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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   MEDLINE=98162722; 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 MASS
RP   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: L-glutamate + H(2)O + NADP(+) = 2-oxoglutarate
CC       + NH(3) + NADPH.
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
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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; -.
DR   HSSP; P24295; 1AUP.
DR   GeneID; 2539147; -.
DR   KEGG; spo:SPCC622.12c; -.
DR   NMPDR; fig|4896.1.peg.522; -.
DR   GeneDB_Spombe; SPCC622.12c; -.
DR   OMA; P78804; RIFTFRV.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000123-MON; -.
DR   BRENDA; 1.4.1.4; 653.
DR   ArrayExpress; P78804; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11606:SF2; GLFV_DH; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; NADP; Oxidoreductase; Phosphoprotein.
FT   CHAIN         1    451       NADP-specific glutamate dehydrogenase.
FT                                /FTId=PRO_0000182794.
FT   ACT_SITE    113    113       By similarity.
FT   MOD_RES     252    252       Phosphoserine.
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
//