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P0A6L0

- DEOC_ECOLI

UniProt

P0A6L0 - DEOC_ECOLI

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Protein

Deoxyribose-phosphate aldolase

Gene

deoC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei167 – 1671Schiff-base intermediate with acetaldehyde1 Publication
Active sitei201 – 20111 Publication

GO - Molecular functioni

  1. deoxyribose-phosphate aldolase activity Source: EcoCyc
  2. lyase activity Source: EcoliWiki

GO - Biological processi

  1. carbohydrate catabolic process Source: EcoliWiki
  2. cellular response to DNA damage stimulus Source: EcoliWiki
  3. deoxyribonucleotide catabolic process Source: EcoliWiki
  4. deoxyribose phosphate catabolic process Source: UniProtKB-UniPathway
  5. nucleobase-containing small molecule interconversion Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciEcoCyc:DEOXYRIBOSE-P-ALD-MONOMER.
ECOL316407:JW4344-MONOMER.
MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER.
SABIO-RKP0A6L0.
UniPathwayiUPA00002; UER00468.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyribose-phosphate aldolase (EC:4.1.2.4)
Short name:
DERA
Alternative name(s):
2-deoxy-D-ribose 5-phosphate aldolase
Phosphodeoxyriboaldolase
Short name:
Deoxyriboaldolase
Gene namesi
Name:deoC
Synonyms:dra, thyR
Ordered Locus Names:b4381, JW4344
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10221. deoC.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 259259Deoxyribose-phosphate aldolasePRO_0000057296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei167 – 1671N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A6L0.
PRIDEiP0A6L0.

2D gel databases

SWISS-2DPAGEP0A6L0.

Expressioni

Gene expression databases

GenevestigatoriP0A6L0.

Interactioni

Subunit structurei

Monomer and homodimer.

Protein-protein interaction databases

IntActiP0A6L0. 8 interactions.
STRINGi511145.b4381.

Structurei

Secondary structure

1
259
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Beta strandi15 – 184Combined sources
Helixi26 – 3510Combined sources
Beta strandi44 – 474Combined sources
Helixi50 – 523Combined sources
Helixi53 – 6210Combined sources
Beta strandi68 – 758Combined sources
Turni76 – 783Combined sources
Helixi83 – 9614Combined sources
Beta strandi99 – 1046Combined sources
Helixi107 – 1115Combined sources
Helixi116 – 13116Combined sources
Beta strandi135 – 1395Combined sources
Helixi142 – 1454Combined sources
Helixi148 – 16013Combined sources
Beta strandi164 – 1674Combined sources
Helixi179 – 19214Combined sources
Turni195 – 1973Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi203 – 2053Combined sources
Helixi209 – 22315Combined sources
Turni230 – 2323Combined sources
Beta strandi235 – 2384Combined sources
Helixi240 – 2489Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JCJX-ray1.10A/B1-259[»]
1JCLX-ray1.05A/B1-259[»]
1KTNX-ray1.40A/B1-250[»]
1P1XX-ray0.99A/B1-259[»]
ProteinModelPortaliP0A6L0.
SMRiP0A6L0. Positions 1-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6L0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0274.
HOGENOMiHOG000241644.
InParanoidiP0A6L0.
KOiK01619.
OMAiCKEACGD.
OrthoDBiEOG6QZMW5.
PhylomeDBiP0A6L0.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00592. DeoC_type2.
InterProiIPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/FbaB/lacD_aldolase.
IPR023649. DeoC_typeII.
[Graphical view]
PANTHERiPTHR10889. PTHR10889. 1 hit.
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFiPIRSF001357. DeoC. 1 hit.
TIGRFAMsiTIGR00126. deoC. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6L0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP
60 70 80 90 100
RFIPIARKTL KEQGTPEIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE
110 120 130 140 150
VDVVFPYRAL MAGNEQVGFD LVKACKEACA AANVLLKVII ETGELKDEAL
160 170 180 190 200
IRKASEISIK AGADFIKTST GKVAVNATPE SARIMMEVIR DMGVEKTVGF
210 220 230 240 250
KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL LASLLKALGH

GDGKSASSY
Length:259
Mass (Da):27,734
Last modified:March 29, 2005 - v1
Checksum:iABA50C625195D494
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181T → N in CAA26974. (PubMed:6749498)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03224 Genomic DNA. Translation: CAA26974.1.
U14003 Genomic DNA. Translation: AAA97277.1.
U00096 Genomic DNA. Translation: AAC77334.1.
AP009048 Genomic DNA. Translation: BAE78370.1.
PIRiA01102. ADECD.
RefSeqiNP_418798.1. NC_000913.3.
YP_492511.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77334; AAC77334; b4381.
BAE78370; BAE78370; BAE78370.
GeneIDi12934356.
948902.
KEGGiecj:Y75_p4265.
eco:b4381.
PATRICi32124378. VBIEscCol129921_4529.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03224 Genomic DNA. Translation: CAA26974.1 .
U14003 Genomic DNA. Translation: AAA97277.1 .
U00096 Genomic DNA. Translation: AAC77334.1 .
AP009048 Genomic DNA. Translation: BAE78370.1 .
PIRi A01102. ADECD.
RefSeqi NP_418798.1. NC_000913.3.
YP_492511.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P0A6L0.
SMRi P0A6L0. Positions 1-250.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0A6L0. 8 interactions.
STRINGi 511145.b4381.

2D gel databases

SWISS-2DPAGE P0A6L0.

Proteomic databases

PaxDbi P0A6L0.
PRIDEi P0A6L0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77334 ; AAC77334 ; b4381 .
BAE78370 ; BAE78370 ; BAE78370 .
GeneIDi 12934356.
948902.
KEGGi ecj:Y75_p4265.
eco:b4381.
PATRICi 32124378. VBIEscCol129921_4529.

Organism-specific databases

EchoBASEi EB0217.
EcoGenei EG10221. deoC.

Phylogenomic databases

eggNOGi COG0274.
HOGENOMi HOG000241644.
InParanoidi P0A6L0.
KOi K01619.
OMAi CKEACGD.
OrthoDBi EOG6QZMW5.
PhylomeDBi P0A6L0.

Enzyme and pathway databases

UniPathwayi UPA00002 ; UER00468 .
BioCyci EcoCyc:DEOXYRIBOSE-P-ALD-MONOMER.
ECOL316407:JW4344-MONOMER.
MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER.
SABIO-RK P0A6L0.

Miscellaneous databases

EvolutionaryTracei P0A6L0.
PROi P0A6L0.

Gene expression databases

Genevestigatori P0A6L0.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00592. DeoC_type2.
InterProi IPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/FbaB/lacD_aldolase.
IPR023649. DeoC_typeII.
[Graphical view ]
PANTHERi PTHR10889. PTHR10889. 1 hit.
Pfami PF01791. DeoC. 1 hit.
[Graphical view ]
PIRSFi PIRSF001357. DeoC. 1 hit.
TIGRFAMsi TIGR00126. deoC. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDEOC_ECOLI
AccessioniPrimary (citable) accession number: P0A6L0
Secondary accession number(s): P00882, Q2M5T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 29, 2005
Last modified: November 26, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3