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G2PNL5 (G2PNL5_MURRD) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length218 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. SAAS SAAS018225 HAMAP-Rule MF_00494

Catalytic activity

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

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. SAAS SAAS018225 HAMAP-Rule MF_00494

Subcellular location

Cytoplasm By similarity SAAS SAAS018225 HAMAP-Rule MF_00494.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site871 By similarity HAMAP-Rule MF_00494

Sequences

Sequence LengthMass (Da)Tools
G2PNL5 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: 87E9146B010BC8E9

FASTA21823,677
        10         20         30         40         50         60 
MKFFIDTANL DQIKEAQELG VLDGVTTNPS LMAKEGITGK DNILKHYVDI CNIVDGDVSA 

        70         80         90        100        110        120 
EVVATDFDGM VKEGEELAEL HEQIVVKVPM IRDGVKALKY FSDKGIRTNC TLVFSPGQAL 

       130        140        150        160        170        180 
LAAKAGANYV SPFLGRLDDI STDGLNLIAE IRLIYDNYGF ETEILAASIR HTMHVIDCAK 

       190        200        210 
LGADVMTGPL SSIDGLLKHP LTDIGLAKFL EDYKKGNS 

« Hide

References

[1]"The complete genome of Muricauda ruestringensis DSM 13258."
Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V. expand/collapse author list , Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13258 / LMG 19739 / B1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002999 Genomic DNA. Translation: AEM72428.1.
RefSeqYP_004789850.1. NC_015945.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEM72428; AEM72428; Murru_3416.
GeneID11056269.
KEGGmrs:Murru_3416.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00616.
OMADNYGFET.

Enzyme and pathway databases

BioCycMRUE886377:GI6V-3462-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 nameG2PNL5_MURRD
AccessionPrimary (citable) accession number: G2PNL5
Entry history
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: April 3, 2013
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)