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Reviewed, UniProtKB/Swiss-Prot Q5PCU4 (TAL2_SALPA)

Last modified November 3, 2009. Version 30. 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 2
    EC=2.2.1.2
Gene names
Name: tal2
Ordered Locus Names: SPA0396
OrganismSalmonella paratyphi A [Complete proteome] [HAMAP]
Taxonomic identifier54388 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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. HAMAP 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 MF_00492

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPentose shunt
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpentose-phosphate shunt

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontransaldolase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Transaldolase 2 HAMAP MF_00492
PRO_0000230970

Sites

Active site1311 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PCU4-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: D7F9B77FDAFD5D15

FASTA31635,538
        10         20         30         40         50         60 
MNQLDGIKQF TTVVADSGDI ESIRHYQPQD ATTNPSLLLK AAGLEQYGHL IEDAIAWGKK 

        70         80         90        100        110        120 
HGGTQEQQVA AASDKLAVNF GAEILKSIPG RVSTEVDARL SFDKEKSIEK ARHLVGLYQQ 

       130        140        150        160        170        180 
QGIDKSRILI KLAATWEGIR AAGQLEKEGI NCNLTLLFSF AQARACAEAG VYLISPFVGR 

       190        200        210        220        230        240 
IYDWYQARSP LEPYVVEEDP GVKSVRNIYD YFKQHRYETI VMGASFRRTE QILALTGCDR 

       250        260        270        280        290        300 
LTISPNLLKE LKEKEEPVIR KLVPSSQMFH RPTSMTEAEF RWEHNQDAMA VEKLSEGIRL 

       310 
FAVDQRKLED LLAAKL 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

CP000026 Genomic DNA. Translation: AAV76407.1.
RefSeqYP_149719.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3176147.
GenomeReviewsGene locus SPA0396 in contig CP000026_GR.
KEGGspt:SPA0396.
NMPDRfig|295319.3.peg.1716.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5PCU4.
OMAGCEILAI.

Enzyme and pathway databases

BioCycSENT295319:SPA0396-MON.

Family and domain databases

HAMAPMF_00492.
[Tree]
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTAL2_SALPA
AccessionPrimary (citable) accession number: Q5PCU4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 4, 2005
Last modified: November 3, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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