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A9HYZ1 (TAL_BORPD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:tal
Ordered Locus Names:Bpet3545
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

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 By similarity HAMAP MF_00492.

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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionsedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Transaldolase HAMAP MF_00492
PRO_1000126236

Sites

Active site1261 By similarity

Sequences

Sequence LengthMass (Da)Tools
A9HYZ1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 4460A220C1B85E10

FASTA31934,736
        10         20         30         40         50         60 
MSSQLEALRR HTTVVADTGD FEAMRALRPT DATTNPSLIL KAVQKEAYRP LLQQVVRDHR 

        70         80         90        100        110        120 
GAPLAELTDR LLVAFGREIL NIVPGRVSTE VDARLSFDTR ATVERGRGLI ALYEAAGIPR 

       130        140        150        160        170        180 
ERVLIKTAST WEGIQAARLL QADGIRCNLT LLFSLPQAVA CADAGVQLIS PFVGRIYDWY 

       190        200        210        220        230        240 
KKAAGADWVE AERAGANDPG VQSVTEIYRY YKRHGITTEI MGASFRNKGQ ILALAGCDLL 

       250        260        270        280        290        300 
TISPELLAEL DGAQGDVPVR LTRDDEAGEV PARRPADEVW FRTELNANAM ATEKLAEGIR 

       310 
LFSADAIKLD ALLGGAAGR

« Hide

References

[1]"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae."
Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. expand/collapse author list , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.
BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM902716 Genomic DNA. Translation: CAP43888.1.
RefSeqYP_001632156.1. NC_010170.1.

3D structure databases

ProteinModelPortalA9HYZ1.
SMRA9HYZ1. Positions 2-314.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9HYZ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5818046.
GenomeReviewsGene locus Bpet3545 in contig AM902716_GR.
KEGGbpt:Bpet3545.
PATRIC21168697. VBIBorPet31633_3583.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG286747.
OMAFINDEPH.
ProtClustDBPRK05269.

Enzyme and pathway databases

BioCycBPET94624:BPET3545-MONOMER.

Family and domain databases

HAMAPMF_00492. Transaldolase_1.
[Tree]
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTAL_BORPD
AccessionPrimary (citable) accession number: A9HYZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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