ID   LYS9_SCHPO              Reviewed;         450 AA.
AC   O59711;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Saccharopine dehydrogenase [NADP+, L-glutamate-forming];
DE            EC=1.5.1.10;
DE   AltName: Full=Saccharopine reductase;
GN   Name=lys9; ORFNames=SPBC3B8.03;
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- CATALYTIC ACTIVITY: N(6)-(L-1,3-dicarboxypropyl)-L-lysine +
CC       NADP(+) + H(2)O = L-glutamate + L-2-aminoadipate 6-semialdehyde +
CC       NADPH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (fungi route): step
CC       2/3.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
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DR   EMBL; CU329671; CAA18292.1; -; Genomic_DNA.
DR   PIR; T40337; T40337.
DR   RefSeq; NP_596411.1; -.
DR   HSSP; Q9P4R4; 1FF9.
DR   GeneID; 2540908; -.
DR   KEGG; spo:SPBC3B8.03; -.
DR   NMPDR; fig|4896.1.peg.2277; -.
DR   GeneDB_Spombe; SPBC3B8.03; -.
DR   OMA; O59711; PYFIYPG.
DR   BRENDA; 1.5.1.10; 653.
DR   ArrayExpress; O59711; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004755; F:saccharopine dehydrogenase (NADP+, L-glutam...; IEA:EC.
DR   GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR005097; Saccharopine_DH.
DR   Pfam; PF03435; Saccharop_dh; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Lysine biosynthesis; NADP; Oxidoreductase.
FT   CHAIN         1    450       Saccharopine dehydrogenase [NADP+, L-
FT                                glutamate-forming].
FT                                /FTId=PRO_0000316856.
SQ   SEQUENCE   450 AA;  49938 MW;  1AEE17A423715C71 CRC64;
     MPSILLLGSG FVAHPTLEYL SRRKENNITV ACRTLSKAEA FINGIPNSKA IALDVNDEAA
     LEKAVSEHDL TISLIPYTYH ATVMKAAIKH GKHVCTTSYV NPKMAELEEA AIKAGSICMN
     EIGVDPGIDH LYAIKTIEEV HKAGGKIKSF LSYCGGLPAP EDSNNPLGYK FSWSSRGVLL
     ALRNSAKFYE NGKLVEIDGK DLMETAKPYF IYPGYAFVCY PNRDSTVYQE RYQIPEAETI
     IRGTLRYQGF PEFIHCLVDM GFLDETAQEY LSPEAPALPW KEVTARVIKA ESSSEADLIK
     KISSIHKFKD EDDKKRILNG LKWLGMFSSK PVTPRGNPLD TLCATLEELM QYEEGERDML
     ILQHKFEVET KEGKRQTRTC TLLDYGVPNG YTSMAKLVGV PCGVATQQIL DGVINTPGVL
     APNDMKLCGP LIDTLAKEGI RLEEEIIDEE
//