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Q65D22 (DEOC2_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2

Short name=DERA 2
EC=4.1.2.4
Alternative name(s):
2-deoxy-D-ribose 5-phosphate aldolase 2
Phosphodeoxyriboaldolase 2
Short name=Deoxyriboaldolase 2
Gene names
Name:deoC2
Synonyms:deoC, dra
Ordered Locus Names:BLi04229, BL00229
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length223 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. HAMAP MF_00114

Catalytic activity

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

Subcellular location

Cytoplasm By similarity HAMAP MF_00114.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processdeoxyribonucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondeoxyribose-phosphate aldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 223223Deoxyribose-phosphate aldolase 2 HAMAP MF_00114
PRO_0000231532

Sites

Active site1521Schiff-base intermediate with acetaldehyde By similarity
Active site1811 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65D22 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 4FDB3D4DE04452AB

FASTA22323,456
        10         20         30         40         50         60 
MTIANLIDHT ALKPHTQKSE IKKLIEEAKA YQFASVCVNP TWVEFAAEEL KGTEIDVCTV 

        70         80         90        100        110        120 
IGFPLGANTT ETKAFETKDA IAKGATEVDM VINIAALKDG NDDFVEADIR AVVEAAKGKA 

       130        140        150        160        170        180 
LVKVIIETCL LTDEEKERAC RLAVAAGADF VKTSTGFSTG GATAEDIALM RKTVGPDIGV 

       190        200        210        220 
KASGGIRTKE DVETMISNGA TRIGASAGVS IVSGAEGKNE DNY 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU43042.1.
CP000002 Genomic DNA. Translation: AAU25663.1.
RefSeqYP_081301.1. NC_006270.3.
YP_093735.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65D22.
SMRQ65D22. Positions 3-218.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65D22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000055542; EBBACP00000054073; EBBACG00000055533.
EBBACT00000060560; EBBACP00000058993; EBBACG00000060551.
GeneID3031406.
3100763.
GenomeReviewsGene locus BLi04229 in contig AE017333_GR.
Gene locus BL00229 in contig CP000002_GR.
KEGGbld:BLi04229.
bli:BL00229.
NMPDRfig|279010.5.peg.3883.
PATRIC18954284. VBIBacLic203714_4317.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0274.
GeneTreeEBGT00050000000908.
HOGENOMHBG636421.
OMAIDHTNLK.
PhylomeDBQ65D22.
ProtClustDBCLSK929138.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI04229-MONOMER.
BLIC279010:BL00229-MONOMER.

Family and domain databases

HAMAPMF_00114. DeoC_type1.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/AroFGH_arch.
IPR022979. Deoxyribose_phosphate_aldo_1.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01619.
PANTHERPTHR10889. DeoC. 1 hit.
PfamPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFPIRSF001357. DeoC. 1 hit.
TIGRFAMsTIGR00126. DeoC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEOC2_BACLD
AccessionPrimary (citable) accession number: Q65D22
Secondary accession number(s): Q62NJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2004
Last modified: January 25, 2012
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families