Skip Header

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

D2QAD8 (D2QAD8_BIFDB) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Protein attributes

Sequence length367 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_00493

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP-Rule 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-Rule MF_00493

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00493.

Sequence similarities

Belongs to the transaldolase family. Type 2 subfamily. HAMAP-Rule MF_00493

Ontologies

Keywords
   Biological processPentose shunt HAMAP-Rule MF_00493
   Cellular componentCytoplasm HAMAP-Rule MF_00493
   Molecular functionTransferase HAMAP-Rule MF_00493 EMBL ADB09774.1
   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_functionsedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1381 By similarity HAMAP-Rule MF_00493

Sequences

Sequence LengthMass (Da)Tools
D2QAD8 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: F3D4B25088BB1E3F

FASTA36739,875
        10         20         30         40         50         60 
MTEATQRTSD SGVSIWLDDL SRTRIESGNL QELIKDKNVV GVTTNPSIFQ KALSQVGPYD 

        70         80         90        100        110        120 
AQLKELGKVD VETAIRELTT TDVRNATDIF REVAEATDFV DGRVSIEVDP RLAHETEATE 

       130        140        150        160        170        180 
KQAVELWEKV NRPNAMIKIP ATLEGLPAIT ATLAKGISVN VTLIFSLERY EQVIDAFIEG 

       190        200        210        220        230        240 
IAQADANGHD LNHIGSVASF FVSRVDTAVD KQLEEIGSDE AKALEGKAAI ANARLAYELF 

       250        260        270        280        290        300 
ENKFANDPRW AALEAKGAKK QRPLWASTGT KNPAYSDCVY VDELVAPFIV NTMPEKTLNA 

       310        320        330        340        350        360 
LADHGNGAPT IKGTYEESHA IMAKLAELGI DFKAVTDKLE ADGVAAFIKS WDSVLTDVQA 


GIDRVNG

« Hide

References

[1]"The Bifidobacterium dentium Bd1 genome sequence reflects its genetic adaptation to the human oral cavity."
Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F., Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A., Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S. expand/collapse author list , Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.
PLoS Genet. 5:E1000785-E1000785(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27534 / DSM 20436 / JCM 1195 / Bd1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001750 Genomic DNA. Translation: ADB09774.1.
RefSeqYP_003360598.1. NC_013714.1.

3D structure databases

ProteinModelPortalD2QAD8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB09774; ADB09774; BDP_1144.
GeneID8691944.
KEGGbde:BDP_1144.
PATRIC31956451. VBIBifDen66312_1088.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000226074.
KOK00616.
OMAINKGAIC.

Enzyme and pathway databases

BioCycBDEN401473:GH09-1114-MONOMER.
UniPathwayUPA00115; UER00414.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00493. Transaldolase_2.
InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004732. Transaldolase_2.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERPTHR10683. PTHR10683. 1 hit.
PfamPF00923. Transaldolase. 1 hit.
[Graphical view]
PIRSFPIRSF036915. Trnald_Bac_Plnt. 1 hit.
TIGRFAMsTIGR00876. tal_mycobact. 1 hit.
PROSITEPS01054. TRANSALDOLASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD2QAD8_BIFDB
AccessionPrimary (citable) accession number: D2QAD8
Entry history
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: May 29, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info