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P34214 (TAL1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. HAMAP-Rule MF_00492

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP-Rule MF_00492

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. HAMAP-Rule MF_00492

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00492

Sequence similarities

Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPentose shunt
   LigandSchiff base
   Molecular functionTransferase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular_functionsedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 334333Transaldolase HAMAP-Rule MF_00492
PRO_0000173570

Sites

Active site1431Schiff-base intermediate with substrate By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P34214 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DD67646509EE7099

FASTA33436,477
        10         20         30         40         50         60 
MSEPSAKKQK FANSLEALKA TGTTVVADTG DFESIAKFTP QDATTNPSLI LAAAKQQAYA 

        70         80         90        100        110        120 
KLIDSAVQYG KKQGQNIDEQ VEIAVDKLLV EFGTAILKVV PGRVSTEVDA RLSFDKDATV 

       130        140        150        160        170        180 
KKALEIIKLY EAEGISKDRV LIKIASTWEG IQAAQELEKE HDIHVNLTLL FSFAQAVAAA 

       190        200        210        220        230        240 
EANVTLISPF VGRILDWYKA STGETYTAET DPGVISVKSI YNYYKKHGYN TIVMGASFRN 

       250        260        270        280        290        300 
VGEIKALAGV DFLTISPKLL DELLSSDEPV AKILDPESAK AEGSERVSFI NDEPKFRFEL 

       310        320        330 
NEDAMATEKL SEGIRKFSAD IVTLFDLIKA KIQA 

« Hide

References

« Hide 'large scale' references
[1]"Transaldolase mutants in the yeast Kluyveromyces lactis provide evidence that glucose can be metabolized through the pentose phosphate pathway."
Jacoby J., Hollenberg C.P., Heinisch J.J.
Mol. Microbiol. 10:867-876(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 76492 / CBS 2359/152 / CLIB 210.
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z17317 Genomic DNA. Translation: CAA78965.1.
CR382121 Genomic DNA. Translation: CAH02703.1.
PIRS39870.
RefSeqXP_451115.1. XM_451115.1.

3D structure databases

ProteinModelPortalP34214.
SMRP34214. Positions 12-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.P34214.

Proteomic databases

PRIDEP34214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2896669.
KEGGkla:KLLA0A02607g.

Phylogenomic databases

eggNOGCOG0176.
HOGENOMHOG000281234.
KOK00616.
OMAAQMPAYQ.
OrthoDBEOG7N905G.

Enzyme and pathway databases

UniPathwayUPA00115; UER00414.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00492. Transaldolase_1.
InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERPTHR10683. PTHR10683. 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_KLULA
AccessionPrimary (citable) accession number: P34214
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways