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Reviewed, UniProtKB/Swiss-Prot O42700 (TAL1_SCHPO)

Last modified November 3, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Transaldolase
    EC=2.2.1.2
Gene names
Name: tal1
ORF Names: SPCC1020.06c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway By similarity.

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.

Sequence similarities

Belongs to the transaldolase family. Type 1 subfamily.

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Ontologies

Keywords
   Biological processPentose shunt
   Molecular functionTransferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpentose-phosphate shunt, non-oxidative branch

Inferred by curator. Source: GeneDB_SPombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_SPombe

nucleus

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functiontransaldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322Transaldolase
PRO_0000173573

Sites

Active site1321 By similarity

Amino acid modifications

Modified residue2681Phosphoserine Ref.3
Modified residue2691Phosphoserine Ref.3

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Sequences

Sequence LengthMass (Da)Tools
O42700-1 [UniParc].

Last modified November 1, 1998. Version 2.
Checksum: 0807DC610EEB2E7E

FASTA32235,238
        10         20         30         40         50         60 
MSSLEQLKAT GTVVVSDTGD FESIAKYKPQ DATTNPSLIL AASKKPQYAA LVDAAVDYAK 

        70         80         90        100        110        120 
AKGGSINSQI EIAFDRLLIE FGTKILAIVP GRVSTEVDAR YSFDTQTTIE KARHLIKLYE 

       130        140        150        160        170        180 
AEGIGRERVL IKIASTYEGI QAAKQLEEEG IHCNLTLLFS FVQAVACAEA NVTLISPFVG 

       190        200        210        220        230        240 
RILDFYKAKN NRDYTAQEDP GVVSVSNIFN YYKKFGYKTI VMGASFRNVG EIKELAGVDF 

       250        260        270        280        290        300 
LTISPALLEQ LNNSTDAVPK KLDASKASSL NLEKVSYLTD EPKFRFDFNN DEMAVVKLST 

       310        320 
GIAAFAKDAD TLRTILKAKL EA

« Hide

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References

« Hide 'large scale' 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: ATCC 38366 / 972.
[2]"S.pombe transaldolase homolog."
Kawamukai M.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 111-322.
[3]"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-268 AND SER-269, MASS SPECTROMETRY.

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Cross-references

Sequence databases

CU329672 Genomic DNA. Translation: CAA18994.1.
AB010049 mRNA. Translation: BAA24182.1.
PIRT40834.
T43308.
RefSeqNP_587953.1.

3D structure databases

HSSPHSSP built from PDB template 1F05 based on UniProtKB P37837.
ModBaseSearch...

Protein-protein interaction databases

STRINGO42700.

Genome annotation databases

GeneID2538977.
GenomeReviewsGene locus tal1 in contig CU329672_GR.
KEGGspo:SPCC1020.06c.
NMPDRfig|4896.1.peg.291.

Organism-specific databases

GeneDB_SpombeSPCC1020.06c.

Phylogenomic databases

OMAEYKPQDA.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-002286-MON.
BRENDA2.2.1.2. 653.

Gene expression databases

ArrayExpressO42700.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_AB.
IPR018225. Transaldolase_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR10683. Transaldolase. 1 hit.
PTHR10683:SF3. Transaldolase_AB. 1 hit.
PfamPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00874. talAB. 1 hit.
PROSITEPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameTAL1_SCHPO
AccessionPrimary (citable) accession number: O42700
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: November 1, 1998
Last modified: November 3, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents