Deoxyribose-phosphate aldolase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P0A6L0 (DEOC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate catabolic process Inferred from direct assay Ref.1. Source: EcoliWiki deoxyribonucleotide catabolic process Inferred from mutant phenotype PubMed 5340684. Source: EcoliWiki deoxyribose phosphate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway nucleobase-containing small molecule interconversion Inferred from mutant phenotype PubMed 5340684. Source: EcoliWiki response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	deoxyribose-phosphate aldolase activity Inferred from direct assay Ref.1. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 259

259

Deoxyribose-phosphate aldolase HAMAP-Rule 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...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6L0 [UniParc].

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

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

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] [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 277:1453-1474(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, 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.

PIR

ADECD. A01102.

RefSeq

NP_418798.1. NC_000913.2.
YP_492511.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0A6L0.

SMR

P0A6L0. Positions 1-250.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6L0. 8 interactions.

STRING

511145.b4381.

2D gel databases

SWISS-2DPAGE

P0A6L0.

Proteomic databases

PaxDb

P0A6L0.

PRIDE

P0A6L0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77334; AAC77334; b4381.
BAE78370; BAE78370; BAE78370.

GeneID

12934356.
948902.

KEGG

ecj:Y75_p4265.
eco:b4381.

PATRIC

32124378. VBIEscCol129921_4529.

Organism-specific databases

EchoBASE

EB0217.

EcoGene

EG10221. deoC.

Phylogenomic databases

eggNOG

COG0274.

HOGENOM

HOG000241644.

K01619.

OMA

PEVRIAT.

ProtClustDB

PRK05283.

Enzyme and pathway databases

BioCyc

EcoCyc:DEOXYRIBOSE-P-ALD-MONOMER.
ECOL316407:JW4344-MONOMER.
MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER.

SABIO-RK

P0A6L0.

UniPathway

UPA00002; UER00468.

Gene expression databases

Genevestigator

P0A6L0.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_00592. DeoC_type2.

InterPro

IPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/FbaB/lacD_aldolase.
IPR023649. DeoC_bac.
[Graphical view]

PANTHER

PTHR10889. PTHR10889. 1 hit.

Pfam

PF01791. DeoC. 1 hit.
[Graphical view]

PIRSF

PIRSF001357. DeoC. 1 hit.

TIGRFAMs

TIGR00126. deoC. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6L0.

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:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents