Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A0LTY8 (TAL_ACIC1)

Last modified November 3, 2009. Version 20. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Transaldolase
    EC=2.2.1.2
Gene names
Name: tal
Ordered Locus Names: Acel_1126
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Acidothermaceae › Acidothermus

Hide | Top

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

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_00493

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_00493

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the transaldolase family. Type 2 subfamily.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Transaldolase HAMAP MF_00493
PRO_1000026519

Sites

Active site1401 By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
A0LTY8-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 9212E2A9C38C83AA

FASTA37240,947
        10         20         30         40         50         60 
MTDPLAELSA AGVSIWIDDI SRDRLQTGNL AALIRDRHVV GVTTNPTIFG KAIEGSARYQ 

        70         80         90        100        110        120 
DQLRDLAVRG VDVNEALRAL TAYDVRWACD VTRPVFDATD GVDGRVSIEV DPRLAHDTEA 

       130        140        150        160        170        180 
TIAEARALWW LVDRPNLFIK IPATVEGLPA IAQCLAEGIS VNVTLIFSVK RYEQVIDAFF 

       190        200        210        220        230        240 
DGVERAIEAG HDLSRLASVA SFFVSRVDTE VDKRLEKIGG EALQWKAKAA VANARLAYRT 

       250        260        270        280        290        300 
YEEKFATPRW QALAAKGARP QRPLWASTST KDPSLPDTLY VTELVAPGTV NTMPESTLQA 

       310        320        330        340        350        360 
VYDHGVIRGD TIRGYYADAQ ATLDALATLG IDYDDVTDTL EREGVEKFEA SWTELAAAVT 

       370 
RSLERARRER GR

« Hide

Hide | Top

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Hide | Top

Cross-references

Sequence databases

CP000481 Genomic DNA. Translation: ABK52898.1.
RefSeqYP_872884.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0LTY8.

Genome annotation databases

GeneID4485182.
GenomeReviewsGene locus Acel_1126 in contig CP000481_GR.
KEGGace:Acel_1126.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMPEKTLD.

Family and domain databases

HAMAPMF_00493.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR004732. Tal_mycobact.
IPR001585. Transaldolase.
IPR018225. Transaldolase_AS.
IPR014634. Transaldolase_Bac/Pln.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR10683. Transaldolase. 1 hit.
PfamPF00923. Transaldolase. 1 hit.
[Graphical view]
PIRSFPIRSF036915. Trnald_Bac_Plnt. 1 hit.
TIGRFAMsTIGR00876. tal_mycobact. 1 hit.
PROSITEPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameTAL_ACIC1
AccessionPrimary (citable) accession number: A0LTY8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: November 3, 2009
This is version 20 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)

Hide | Top

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