Deoxyribose-phosphate aldolase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A6L0 (DEOC_ECOLI)

Last modified November 3, 2009. Version 46. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Deoxyribose-phosphate aldolase
    EC=4.1.2.4
Alternative name(s):
    Phosphodeoxyriboaldolase
      Short name=Deoxyriboaldolase
      Short name=DERA

Gene names

Name:	deoC
Synonyms:	dra, thyR
Ordered Locus Names:	b4381, JW4344

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. HAMAP 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 MF_00592
Subunit structure	Monomer and homodimer. HAMAP MF_00592
Subcellular location	Cytoplasm. HAMAP MF_00592
Sequence similarities	Belongs to the deoC/fbaB aldolase family. DeoC type 2 subfamily.

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Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate catabolic process Inferred from electronic annotation. Source: HAMAP deoxyribonucleotide catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	deoxyribose-phosphate aldolase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 259

259

Deoxyribose-phosphate aldolase HAMAP MF_00592

PRO_0000057296

Sites

Active site

167

Schiff-base intermediate with acetaldehyde Ref.6

Active site

201

Ref.6

Amino acid modifications

Modified residue

167

N6-acetyllysine Ref.5

Experimental info

Sequence conflict

T → N in CAA26974. Ref.1

Secondary structure

259

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A6L0-1 [UniParc].

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

259

27,734

        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

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References

	« Hide 'large scale' referencesShow '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: 6749498] [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: 7610040] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167, MASS SPECTROMETRY.
[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: 11598300] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS), ACTIVE SITE, MUTAGENESIS.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X03224 Genomic DNA. Translation: CAA26974.1.
U14003 Genomic DNA. Translation: AAA97277.1.
U00096 Genomic DNA. Translation: AAC77334.1.
AP009048 Genomic DNA. Translation: BAE78370.1.

PIR

ADECD. A01102.

RefSeq

AP_004869.1.
NP_418798.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JCJ	X-ray	1.10	A/B	1-259	[»]
1JCL	X-ray	1.05	A/B	1-259	[»]
1KTN	X-ray	1.40	A/B	1-250	[»]
1P1X	X-ray	0.99	A/B	1-259	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6L0. 8 interactions.

STRING

P0A6L0.

2-D gel databases

SWISS-2DPAGE

P0A6L0.

Genome annotation databases

GeneID

948902.

GenomeReviews

Gene locus JW4344 in contig AP009048_GR.
Gene locus b4381 in contig U00096_GR.

KEGG

ecj:JW4344.
eco:b4381.

Organism-specific databases

EchoBASE

EB0217.

EcoGene

EG10221. deoC.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A6L0.

OMA

CKEACGD.

Enzyme and pathway databases

BioCyc

EcoCyc:DEOXYRIBOSE-P-ALD-MON.
MetaCyc:DEOXYRIBOSE-P-ALD-MON.

Gene expression databases

Genevestigator

P0A6L0.

Family and domain databases

HAMAP

MF_00592.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/AroFGH_arch.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR10889. DeoC. 1 hit.

Pfam

PF01791. DeoC. 1 hit.
[Graphical view]

PIRSF

PIRSF001357. DeoC. 1 hit.

TIGRFAMs

TIGR00126. deoC. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

DEOC_ECOLI

Accession

Primary (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:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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