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Reviewed, UniProtKB/Swiss-Prot P17440 (TAL1_PICJA)

Last modified May 5, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Transaldolase-1
    EC=2.2.1.2
Alternative name(s):
    Transaldolase I
OrganismPichia jadinii (Yeast) (Candida utilis)
Taxonomic identifier4903 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaePichia

Protein attributes

Sequence length9 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

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
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processpentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiontransaldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›9›9Transaldolase-1
PRO_0000173571

Experimental info

Non-terminal residue11
Non-terminal residue91

Sequences

Sequence LengthMass (Da)Tools
P17440-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 274F31AF0EB1E058

FASTA91,008
HGIHCBTLL 

« Hide

References

[1]"Purification of crystallization of transaldolase isozyme I and evidence for different genetic origin of isozymes I and III in Candida utilis."
Sun S.C., Joris L., Tsolas O.
Arch. Biochem. Biophys. 178:69-78(1977) [PubMed: 556924] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRA12872.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA2.2.1.2. 288941.

Family and domain databases

InterProIPR018225. Transaldolase_AS.
[Graphical view]
PROSITEPS01054. TRANSALDOLASE_1. Partial match.
PS00958. TRANSALDOLASE_2. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTAL1_PICJA
AccessionPrimary (citable) accession number: P17440
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 5, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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