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A5J9H5 (A5J9H5_BURMA) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 26. 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 names
EC=4.1.2.4 EMBL EDK52991.1
Gene names
Name:deoC EMBL EDK52991.1
ORF Names:BMAFMH_K0040 EMBL EDK52991.1
OrganismBurkholderia mallei FMH EMBL EDK52991.1
Taxonomic identifier334802 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate By similarity. SAAS SAAS011343

Catalytic activity

2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. SAAS SAAS011343

Pathway

Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. SAAS SAAS011343

Ontologies

Keywords
   LigandSchiff base SAAS SAAS011343
   Molecular functionLyase SAAS SAAS011343 EMBL EDK52991.1
Gene Ontology (GO)
   Biological processdeoxyribonucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functiondeoxyribose-phosphate aldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
A5J9H5 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 43B63E7042F8C3EE

FASTA26026,964
        10         20         30         40         50         60 
MELSLNRNQL TEAALKALHL IDLTSLNDDD TEERIASLAA SADTPVGTPA ALCVYPRFVG 

        70         80         90        100        110        120 
AAHAALARHG LVLPVATVTN FPHGAADPDA AARETADALA RGADEIDVVF PYRALIDGDE 

       130        140        150        160        170        180 
RVGRELVAQC RAAAGAQCLK VILETGELRD AAAIRRASEI AIEEGADFLK TSTGKVAVNA 

       190        200        210        220        230        240 
TLDAAAAMLA TIRVAGRMVG FKAAGGVRTA QDAAQYLSLA QRELGPGYLT SATFRFGASG 

       250        260 
LLGNLLETLG HRAGATRGAY 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: FMH EMBL EDK52991.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS264098 Genomic DNA. Translation: EDK52991.1.

3D structure databases

ProteinModelPortalA5J9H5.
SMRA5J9H5. Positions 9-251.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC26918077. VBIBurMal45758_4114.

Phylogenomic databases

OMAFELVKQC.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/AroFGH_arch.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR10889. DeoC. 1 hit.
PfamPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFPIRSF001357. DeoC. 1 hit.
TIGRFAMsTIGR00126. DeoC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA5J9H5_BURMA
AccessionPrimary (citable) accession number: A5J9H5
Entry history
Integrated into UniProtKB/TrEMBL: June 26, 2007
Last sequence update: June 26, 2007
Last modified: December 14, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)