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O42700 (TAL1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. 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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Names and origin

Protein namesRecommended name:
Transaldolase

EC=2.2.1.2
Gene names
Name:tal1
ORF Names:SPCC1020.06c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Ontologies

Keywords
   Biological processPentose shunt
   Molecular functionTransferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference 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 functionsedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase 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 – 322322Transaldolase
PRO_0000173573

Sites

Active site1321 By similarity

Amino acid modifications

Modified residue2681Phosphoserine Ref.3
Modified residue2691Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
O42700 [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

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: 972 / ATCC 24843.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAA18994.1.
AB010049 mRNA. Translation: BAA24182.1.
PIRT40834.
T43308.
RefSeqNP_587953.1. NM_001022944.1.

3D structure databases

ProteinModelPortalO42700.
SMRO42700. Positions 2-321.
ModBaseSearch...

Protein-protein interaction databases

STRINGO42700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1020.06c.1; SPCC1020.06c.1:pep; SPCC1020.06c.
GeneID2538977.
GenomeReviewsGene locus tal1 in contig CU329672_GR.
KEGGspo:SPCC1020.06c.
NMPDRfig|4896.1.peg.291.

Organism-specific databases

GeneDB_SpombeSPCC1020.06c.

Phylogenomic databases

eggNOGfuNOG07388.
GeneTreeEFGT00050000004933.
HOGENOMHBG286747.
OMADTGDFHA.
OrthoDBEOG4XWK6K.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-002286-MONOMER.

Gene expression databases

ArrayExpressO42700.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00616.
PANTHERPTHR10683. Transaldolase. 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...

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: December 14, 2011
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