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Q09694 (LYS1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Saccharopine dehydrogenase [NAD+, L-lysine-forming]
Short name=SDH
EC=1.5.1.7
Alternative name(s):
Lysine--2-oxoglutarate reductase
Gene names
Name:lys3
ORF Names:SPAC227.18, SPAC2F7.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH.

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.

Sequence similarities

Belongs to the AlaDH/PNT family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processlysine biosynthetic process via aminoadipic acid

Inferred from mutant phenotype. Source: GeneDB_Spombe

   Cellular componentcytoplasm

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionsaccharopine dehydrogenase (NAD+, L-lysine-forming) activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 368368Saccharopine dehydrogenase [NAD+, L-lysine-forming]
PRO_0000199014

Sites

Active site2051 By similarity

Amino acid modifications

Modified residue851Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q09694 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 789AB01DB171ED13

FASTA36841,393
        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

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
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. expand/collapse author list , 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.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB61467.1.
PIRS58145. T38549.
T50174.
RefSeqNP_592972.1. NM_001018372.1.

3D structure databases

ProteinModelPortalQ09694.
SMRQ09694. Positions 3-365.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4694154.
STRINGQ09694.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC227.18.1; SPAC227.18.1:pep; SPAC227.18.
GeneID2541500.
GenomeReviewsGene locus lys3 in contig CU329670_GR.
KEGGspo:SPAC227.18.
NMPDRfig|4896.1.peg.2942.

Organism-specific databases

GeneDB_SpombeSPAC227.18.

Phylogenomic databases

eggNOGfuNOG07631.
GeneTreeEFGT00050000005648.
HOGENOMHBG331053.
OMAQFAHCYK.
OrthoDBEOG408RHS.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-001980-MONOMER.

Gene expression databases

ArrayExpressQ09694.

Family and domain databases

InterProIPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
[Graphical view]
KOK00290.
PfamPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]
SMARTSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYS1_SCHPO
AccessionPrimary (citable) accession number: Q09694
Secondary accession number(s): Q9UTC1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 1, 2000
Last modified: January 25, 2012
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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