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B9MDC2 (TAL_ACIET) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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 namesRecommended name:
Transaldolase

EC=2.2.1.2
Gene names
Name:tal
Ordered Locus Names:Dtpsy_0674
OrganismAcidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)) [Complete proteome] [HAMAP]
Taxonomic identifier535289 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length316 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-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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00492.

Sequence similarities

Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Transaldolase HAMAP-Rule MF_00492
PRO_1000198453

Sites

Active site1251Schiff-base intermediate with substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B9MDC2 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 80DA983924EA5258

FASTA31634,486
        10         20         30         40         50         60 
MNQLDALKQY TTVVADTGDF KQLAQFQPQD ATTNPSLILK AVQKPEYAPL LKDCVTRWHG 

        70         80         90        100        110        120 
RAIDELMDRL IVRFGCEILS IIPGRVSTEV DARLSFDTAA TVARAERIVE LYQAEGLHID 

       130        140        150        160        170        180 
RVLIKIAATW EGIQAARQLE QRGIHTNLTL LFSFAQAVAC GQAKVQLISP FVGRIYDWYK 

       190        200        210        220        230        240 
KQAGANWDEA AMAGANDPGV QSVRAIYNHY KHFGIGTEVM GASFRNTGQI VALAGCDLLT 

       250        260        270        280        290        300 
IAPELLAQLA ASDAPVARVL DPEAARRVAL QPVQYDEAGF RYALNADAMA TEKLAEGIRA 

       310 
FAADAAKLEQ LMQAAA 

« Hide

References

[1]"Complete sequence of Diaphorobacter sp. TPSY."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TPSY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001392 Genomic DNA. Translation: ACM32154.1.
RefSeqYP_002552154.1. NC_011992.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING535289.Dtpsy_0674.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM32154; ACM32154; Dtpsy_0674.
GeneID7384179.
KEGGdia:Dtpsy_0674.
PATRIC21778363. VBIDiaSp55748_0696.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0176.
HOGENOMHOG000281234.
KOK00616.
OMAIRLFAID.
OrthoDBEOG6G7R4D.
ProtClustDBPRK05269.

Enzyme and pathway databases

BioCycAEBR535289:GHOO-676-MONOMER.
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 nameTAL_ACIET
AccessionPrimary (citable) accession number: B9MDC2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways