ID   LYS1_SCHPO              Reviewed;         368 AA.
AC   Q09694; Q9UTC1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Saccharopine dehydrogenase [NAD+, L-lysine-forming];
DE            Short=SDH;
DE            EC=1.5.1.7;
DE   AltName: Full=Lysine--2-oxoglutarate reductase;
GN   Name=lys3; ORFNames=SPAC227.18, SPAC2F7.01;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, 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: N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+)
CC       + H(2)O = L-lysine + 2-oxoglutarate + NADH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (fungi route): step
CC       3/3.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
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DR   EMBL; CU329670; CAB61467.1; -; Genomic_DNA.
DR   PIR; T38549; S58145.
DR   PIR; T50174; T50174.
DR   RefSeq; NP_592972.1; -.
DR   GeneID; 2541500; -.
DR   KEGG; spo:SPAC227.18; -.
DR   NMPDR; fig|4896.1.peg.2942; -.
DR   GeneDB_Spombe; SPAC227.18; -.
DR   OMA; Q09694; IGALGRC.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-001980-MON; -.
DR   BRENDA; 1.5.1.7; 653.
DR   ArrayExpress; Q09694; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB_SPombe.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0004754; F:saccharopine dehydrogenase (NAD+, L-lysine-...; IEA:EC.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic...; IMP:GeneDB_SPombe.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR007698; Ala_DH/PNT_C.
DR   InterPro; IPR007886; Ala_DH/PNT_N.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Complete proteome; Lysine biosynthesis; NAD;
KW   Oxidoreductase; Phosphoprotein.
FT   CHAIN         1    368       Saccharopine dehydrogenase [NAD+, L-
FT                                lysine-forming].
FT                                /FTId=PRO_0000199014.
FT   ACT_SITE    205    205       By similarity.
FT   MOD_RES      85     85       Phosphoserine.
SQ   SEQUENCE   368 AA;  41393 MW;  789AB01DB171ED13 CRC64;
     MVAPHLWLRA ETKPLEERSA LTPRTAKILA DAGFQITIER SSQRAFKDKE FERLGFPMVP
     EGSWRHAPKD AYIIGLKELP ENDNSPLKHT HIQFAHCYKN QEGWREVLSR FPAGNGLLYD
     LEFLQDDNGR RVAAFGYHAG FAGSAISCLV WAHQLLHPNK QFPAIRPFPN EKSLVRHVAR
     QVRLALKKNN NQYPRILVIG ALGRCGTGAC DLASKIGIPF DNILRWDINE TKKGGPFTEI
     TESDIFVNCI YLSMPIPKFC TVESLNVPNR KLRVVCDVSC DTTNPNNPIP IYNVNTTFDH
     PTVEVKGVTT PPPLEVISID HLPTLLPRES SEAFSEALIP SLLALKDVDN APVWVRAKKL
     YETMVQKL
//