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Q1LU10 (TAL_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:BCI_0076
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length317 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 – 317317Transaldolase HAMAP MF_00492
PRO_1000014484

Sites

Active site1311 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LU10 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: B96A4251ADE3A3F7

FASTA31736,294
        10         20         30         40         50         60 
MNQLESLKQF TTIVADSGDI ELIRHYTPQD TTTNPSLILK ATSLSYYQNM LEDVLAYARK 

        70         80         90        100        110        120 
QSGNHNAKMR AASDKLAVNI GLEILKIIPG RISTEIDARF SFNSDMCINH AHKIVSLYQE 

       130        140        150        160        170        180 
QGINKSRVLI KLASTWEGIK AAEELEKAGI NCNLTLIFSF AQARACAEAN VYLISPFVGR 

       190        200        210        220        230        240 
IYDWYNQRKL LTEDSYDRED PGVKSVHKIY DYYKQHRYQT IVMGASFRKI DQILALAGCD 

       250        260        270        280        290        300 
YLTISPVLLE KLRSSYQHVE RQLFPATKFF HKPIPLSESQ FRWEHNQDAM AVDQLADGIR 

       310 
KFALDQYNIE KILAKKL 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF13893.1.
RefSeqYP_588554.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LU10.
SMRQ1LU10. Positions 2-317.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LU10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056478.
GenomeReviewsGene locus BCI_0076 in contig CP000238_GR.
KEGGbci:BCI_0076.
PATRIC21073641. VBIBauCic75062_0077.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0176.
HOGENOMHBG286747.
OMAEKERINC.
PhylomeDBQ1LU10.
ProtClustDBPRK12346.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0076-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. False negative.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTAL_BAUCH
AccessionPrimary (citable) accession number: Q1LU10
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 39 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