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Q1LLK8 (TAL_RALME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:Rmet_2089
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length318 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 – 318318Transaldolase HAMAP MF_00492
PRO_1000014517

Sites

Active site1261 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LLK8 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 22FB34901FE6586B

FASTA31834,919
        10         20         30         40         50         60 
MNELEQLRQF TTVVADTGDF QLMKQYKPQD ATTNPSLIFK AVQKPEYRPL LEQAVRDHHG 

        70         80         90        100        110        120 
NSGLDGVMDQ LLIAFGCEIL AIVPGRVSTE VDARLSFDTE ATVAKARHLI GLYEQRGVAR 

       130        140        150        160        170        180 
ERVLIKIAST WEGIRAAEVL QRENIRCNMT LLFSLAQAVA CAEAGAQLIS PFVGRILDWY 

       190        200        210        220        230        240 
KKQAGEKWDP VANGGENDPG VRSVRQIYDY YKKFGYATEV MGASFRGTDQ ILSLAGCDLL 

       250        260        270        280        290        300 
TISPELLEQL AGGQSAVALK LSVEQAQAGN VARIAADEPA FRWQLNEDAM ATEKLSEGIR 

       310 
LFAADAVKLE KLVGELAS

« Hide

References

[1]"Complete sequence of the chromosome of Ralstonia metallidurans CH34."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH34 / ATCC 43123 / DSM 2839.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000352 Genomic DNA. Translation: ABF08968.1.
RefSeqYP_584237.1. NC_007973.1.

3D structure databases

ProteinModelPortalQ1LLK8.
SMRQ1LLK8. Positions 2-315.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LLK8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4038896.
GenomeReviewsGene locus Rmet_2089 in contig CP000352_GR.
KEGGrme:Rmet_2089.
PATRIC20288802. VBIRalMet4734_2498.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0176.
HOGENOMHBG286747.
OMAGCEILAI.
PhylomeDBQ1LLK8.
ProtClustDBPRK05269.

Enzyme and pathway databases

BioCycRMET266264:RMET_2089-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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTAL_RALME
AccessionPrimary (citable) accession number: Q1LLK8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 37 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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