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P0A6L0 (DEOC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms:dra, thyR
Ordered Locus Names:b4381, JW4344
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length259 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. HAMAP-Rule MF_00592

Catalytic activity

2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. HAMAP-Rule MF_00592

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_00592

Subunit structure

Monomer and homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00592.

Sequence similarities

Belongs to the DeoC/FbaB aldolase family. DeoC type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 259259Deoxyribose-phosphate aldolase HAMAP-Rule MF_00592
PRO_0000057296

Sites

Active site1671Schiff-base intermediate with acetaldehyde Ref.6
Active site2011 Ref.6

Amino acid modifications

Modified residue1671N6-acetyllysine Ref.5

Experimental info

Sequence conflict181T → N in CAA26974. Ref.1

Secondary structure

............................................... 259
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6L0 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: ABA50C625195D494

FASTA25927,734
        10         20         30         40         50         60 
MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP RFIPIARKTL 

        70         80         90        100        110        120 
KEQGTPEIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE VDVVFPYRAL MAGNEQVGFD 

       130        140        150        160        170        180 
LVKACKEACA AANVLLKVII ETGELKDEAL IRKASEISIK AGADFIKTST GKVAVNATPE 

       190        200        210        220        230        240 
SARIMMEVIR DMGVEKTVGF KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL 

       250 
LASLLKALGH GDGKSASSY 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of Escherichia coli K12 2-deoxyribose 5-phosphate aldolase. Nucleotide sequence of the deoC gene and the amino acid sequence of the enzyme."
Valentin-Hansen P., Boetius F., Hammer-Jespersen K., Svendsen I.
Eur. J. Biochem. 125:561-566(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[6]"Observation of covalent intermediates in an enzyme mechanism at atomic resolution."
Heine A., DeSantis G., Luz J.G., Mitchell M., Wong C.-H., Wilson I.A.
Science 294:369-374(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS), ACTIVE SITE, MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03224 Genomic DNA. Translation: CAA26974.1.
U14003 Genomic DNA. Translation: AAA97277.1.
U00096 Genomic DNA. Translation: AAC77334.1.
AP009048 Genomic DNA. Translation: BAE78370.1.
PIRADECD. A01102.
RefSeqNP_418798.1. NC_000913.3.
YP_492511.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JCJX-ray1.10A/B1-259[»]
1JCLX-ray1.05A/B1-259[»]
1KTNX-ray1.40A/B1-250[»]
1P1XX-ray0.99A/B1-259[»]
ProteinModelPortalP0A6L0.
SMRP0A6L0. Positions 1-250.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A6L0. 8 interactions.
STRING511145.b4381.

2D gel databases

SWISS-2DPAGEP0A6L0.

Proteomic databases

PaxDbP0A6L0.
PRIDEP0A6L0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77334; AAC77334; b4381.
BAE78370; BAE78370; BAE78370.
GeneID12934356.
948902.
KEGGecj:Y75_p4265.
eco:b4381.
PATRIC32124378. VBIEscCol129921_4529.

Organism-specific databases

EchoBASEEB0217.
EcoGeneEG10221. deoC.

Phylogenomic databases

eggNOGCOG0274.
HOGENOMHOG000241644.
KOK01619.
OMACKEACGD.
OrthoDBEOG6QZMW5.
PhylomeDBP0A6L0.

Enzyme and pathway databases

BioCycEcoCyc:DEOXYRIBOSE-P-ALD-MONOMER.
ECOL316407:JW4344-MONOMER.
MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER.
SABIO-RKP0A6L0.
UniPathwayUPA00002; UER00468.

Gene expression databases

GenevestigatorP0A6L0.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00592. DeoC_type2.
InterProIPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/FbaB/lacD_aldolase.
IPR023649. DeoC_typeII.
[Graphical view]
PANTHERPTHR10889. PTHR10889. 1 hit.
PfamPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFPIRSF001357. DeoC. 1 hit.
TIGRFAMsTIGR00126. deoC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A6L0.
PROP0A6L0.

Entry information

Entry nameDEOC_ECOLI
AccessionPrimary (citable) accession number: P0A6L0
Secondary accession number(s): P00882, Q2M5T6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 29, 2005
Last modified: May 14, 2014
This is version 87 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene