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A0QLL2 (DEOC_MYCA1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyribose-phosphate aldolase

Short name=DERA
EC=4.1.2.4
Alternative name(s):
2-deoxy-D-ribose 5-phosphate aldolase
Phosphodeoxyriboaldolase
Short name=Deoxyriboaldolase
Gene names
Name:deoC
Ordered Locus Names:MAV_4672
OrganismMycobacterium avium (strain 104) [Complete proteome] [HAMAP]
Taxonomic identifier243243 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_00114

Catalytic activity

2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. HAMAP-Rule MF_00114

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. HAMAP-Rule MF_00114

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00114.

Sequence similarities

Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processcarbohydrate catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

deoxyribonucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

deoxyribose phosphate catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondeoxyribose-phosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 223223Deoxyribose-phosphate aldolase HAMAP-Rule MF_00114
PRO_1000015324

Sites

Active site1581Schiff-base intermediate with acetaldehyde By similarity
Active site1881 By similarity

Secondary structure

........................................ 223
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A0QLL2 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 33A436559EB7FC1A

FASTA22321,723
        10         20         30         40         50         60 
MTPTRAQLAA FVDHTLLKPE ATAADVAALV TEAAELGVYA VCVSPPMVPA AVQAGAGVRV 

        70         80         90        100        110        120 
ASVAGFPSGK HVSAVKAHEA ALAVASGAAE IDMVIDVGAA LAGDLDGVRA DIAAVRGAVG 

       130        140        150        160        170        180 
GAVLKVIVES SALLALADEH TLVRVCRAAE DAGADFVKTS TGFHPSGGAS VRAVALMAEA 

       190        200        210        220 
VGGRLGVKAS GGIRTAADAL AMLDAGATRL GLSGTRAVLD GLG 

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 104.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000479 Genomic DNA. Translation: ABK67136.1.
RefSeqYP_883800.1. NC_008595.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3NG3X-ray2.15A/B/C/D1-223[»]
ProteinModelPortalA0QLL2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243243.MAV_4672.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK67136; ABK67136; MAV_4672.
GeneID4528214.
KEGGmav:MAV_4672.
PATRIC17991042. VBIMycAvi38287_4590.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0274.
HOGENOMHOG000241645.
KOK01619.
OMAFENDYLQ.
OrthoDBEOG6QZMW5.
ProtClustDBPRK00507.

Enzyme and pathway databases

BioCycMAVI243243:GH3Y-4672-MONOMER.
UniPathwayUPA00002; UER00468.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00114. DeoC_type1.
InterProIPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/FbaB/lacD_aldolase.
IPR028581. DeoC_typeI.
[Graphical view]
PANTHERPTHR10889. PTHR10889. 1 hit.
PfamPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFPIRSF001357. DeoC. 1 hit.
TIGRFAMsTIGR00126. deoC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceA0QLL2.

Entry information

Entry nameDEOC_MYCA1
AccessionPrimary (citable) accession number: A0QLL2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways