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E6VZD4 (E6VZD4_DESAO) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length215 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_00494 SAAS SAAS018225

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP-Rule MF_00494 SAAS SAAS018225

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_00494 SAAS SAAS018225

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00494 SAAS SAAS018225.

Sequence similarities

Belongs to the transaldolase family. Type 3B subfamily. HAMAP-Rule MF_00494

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site831Schiff-base intermediate with substrate By similarity HAMAP-Rule MF_00494

Sequences

Sequence LengthMass (Da)Tools
E6VZD4 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: 1B12F0EAF5B2B149

FASTA21523,369
        10         20         30         40         50         60 
MQFFLDTANV DQIREVQGLG LLDGVTTNPT LLARQGGDWR EQASLICSMV DGPVSLEVIA 

        70         80         90        100        110        120 
TTHEEMIKEA KDLVSFGENV VVKIPMIAEG LRAMRELGER GIRVNATLVF SPAQALLAAK 

       130        140        150        160        170        180 
LGATYVSPFV GRLDGLSQSG MECVEQIRTI FDNYDFKTQI LVASVRHPMH VLDAALIGAD 

       190        200        210 
VVTLPYATLA QLIRHPLTDS GLAAFLADWE AFQKG 

« Hide

References

[1]"Complete sequence of Desulfovibrio aespoeensis Aspo-2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pedersen K., Jagevall S., Hazen T., Woyke T.
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700646 / DSM 10631 / Aspo-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002431 Genomic DNA. Translation: ADU64006.1.
RefSeqYP_004122752.1. NC_014844.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADU64006; ADU64006; Daes_3013.
GeneID10097642.
KEGGdas:Daes_3013.
PATRIC45206149. VBIDesAes51796_3061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000226073.
KOK00616.

Enzyme and pathway databases

BioCycDAES643562:GH9Z-3071-MONOMER.
UniPathwayUPA00115; UER00414.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00494. Transaldolase_3b.
InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004731. Transaldolase_3A/3B.
IPR022999. Transaldolase_3B.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERPTHR10683. PTHR10683. 1 hit.
PfamPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00875. fsa_talC_mipB. 1 hit.
PROSITEPS01054. TRANSALDOLASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE6VZD4_DESAO
AccessionPrimary (citable) accession number: E6VZD4
Entry history
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: February 19, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)