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UniProtKB/Swiss-Prot entry Q09694


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LYS1_SCHPO
Primary accession number Q09694
Secondary accession number Q9UTC1
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 61)
Name and origin of the protein
Protein name Saccharopine dehydrogenase [NAD+, L-lysine-forming]
Synonyms SDH
EC 1.5.1.7
Lysine--2-oxoglutarate reductase
Gene name
Name: lys3
ORFNames: SPAC227.18, SPAC2F7.01
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CU329670; CAB61467.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T38549; S58145.
T50174; T50174.
RefSeq NP_592972.1; -.
3D structure databases
ModBase Q09694.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-001980-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC227.18; -.
Gene expression databases
ArrayExpress Q09694; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from GeneDB_SPombe).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0004754; Molecular function: saccharopine dehydrogenase (NAD+, L-lysine-forming) activity (inferred from electronic annotation from EC).
GO:0019878; Biological process: lysine biosynthetic process via aminoadipic acid (inferred from mutant phenotype from GeneDB_SPombe).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR007698; Ala_DHase/PNT_C.
IPR007886; Ala_DHase/PNT_N.
Graphical view of domain structure.
Pfam PF01262; AlaDh_PNT_C; 1.
PF05222; AlaDh_PNT_N; 1.
Pfam graphical view of domain structure.
ProtoNet Q09694.
Genome annotation databases
GeneID 2541500; -.
KEGG spo:SPAC227.18; -.
NMPDR fig|4896.1.peg.2942; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Lysine biosynthesis; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   368  368     Saccharopine dehydrogenase [NAD+, L-lysine-forming]. PRO_0000199014
ACT_SITE   205   205        By similarity. 
MOD_RES   85    85        Phosphoserine. 
Sequence information
Length: 368 AA [This is the length of the unprocessed precursor] Molecular weight: 41393 Da [This is the MW of the unprocessed precursor] CRC64: 789AB01DB171ED13 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVAPHLWLRA ETKPLEERSA LTPRTAKILA DAGFQITIER SSQRAFKDKE FERLGFPMVP 

        70         80         90        100        110        120 
EGSWRHAPKD AYIIGLKELP ENDNSPLKHT HIQFAHCYKN QEGWREVLSR FPAGNGLLYD 

       130        140        150        160        170        180 
LEFLQDDNGR RVAAFGYHAG FAGSAISCLV WAHQLLHPNK QFPAIRPFPN EKSLVRHVAR 

       190        200        210        220        230        240 
QVRLALKKNN NQYPRILVIG ALGRCGTGAC DLASKIGIPF DNILRWDINE TKKGGPFTEI 

       250        260        270        280        290        300 
TESDIFVNCI YLSMPIPKFC TVESLNVPNR KLRVVCDVSC DTTNPNNPIP IYNVNTTFDH 

       310        320        330        340        350        360 
PTVEVKGVTT PPPLEVISID HLPTLLPRES SEAFSEALIP SLLALKDVDN APVWVRAKKL 


YETMVQKL 

Q09694 in FASTA format

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