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Protein

Deoxyribose-phosphate aldolase

Gene

deoC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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: 2-deoxy-D-ribose 1-phosphate degradation

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Deoxyribose-phosphate aldolase (deoC)
This subpathway is part of the pathway 2-deoxy-D-ribose 1-phosphate degradation, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate, the pathway 2-deoxy-D-ribose 1-phosphate degradation and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei167Schiff-base intermediate with acetaldehyde1 Publication1
Active sitei2011 Publication1

GO - Molecular functioni

  • deoxyribose-phosphate aldolase activity Source: EcoCyc
  • lyase activity Source: EcoliWiki

GO - Biological processi

  • carbohydrate catabolic process Source: EcoliWiki
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • deoxyribonucleotide catabolic process Source: EcoliWiki
  • deoxyribose phosphate catabolic process Source: UniProtKB-UniPathway
  • 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.
BRENDAi4.1.2.4. 2026.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10221. deoC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000572961 – 259Deoxyribose-phosphate aldolaseAdd BLAST259

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei167N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A6L0.
PaxDbiP0A6L0.
PRIDEiP0A6L0.

2D gel databases

SWISS-2DPAGEP0A6L0.

Interactioni

Subunit structurei

Monomer and homodimer.

Protein-protein interaction databases

BioGridi4263350. 9 interactors.
IntActiP0A6L0. 8 interactors.
STRINGi511145.b4381.

Structurei

Secondary structure

1259
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 12Combined sources10
Beta strandi15 – 18Combined sources4
Helixi26 – 35Combined sources10
Beta strandi44 – 47Combined sources4
Helixi50 – 52Combined sources3
Helixi53 – 62Combined sources10
Beta strandi68 – 75Combined sources8
Turni76 – 78Combined sources3
Helixi83 – 96Combined sources14
Beta strandi99 – 104Combined sources6
Helixi107 – 111Combined sources5
Helixi116 – 131Combined sources16
Beta strandi135 – 139Combined sources5
Helixi142 – 145Combined sources4
Helixi148 – 160Combined sources13
Beta strandi164 – 167Combined sources4
Beta strandi171 – 174Combined sources4
Helixi179 – 192Combined sources14
Turni195 – 197Combined sources3
Beta strandi199 – 201Combined sources3
Beta strandi203 – 205Combined sources3
Helixi209 – 223Combined sources15
Turni230 – 232Combined sources3
Beta strandi235 – 238Combined sources4
Helixi240 – 248Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JCJX-ray1.10A/B1-259[»]
1JCLX-ray1.05A/B1-259[»]
1KTNX-ray1.40A/B1-250[»]
1P1XX-ray0.99A/B1-259[»]
5EKYX-ray1.10A1-259[»]
5EL1X-ray1.25A1-259[»]
5EMUX-ray1.50A1-259[»]
ProteinModelPortaliP0A6L0.
SMRiP0A6L0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6L0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105FCI. Bacteria.
COG0274. LUCA.
HOGENOMiHOG000241644.
InParanoidiP0A6L0.
KOiK01619.
OMAiKIATVTN.
PhylomeDBiP0A6L0.

Family and domain databases

CDDicd00959. DeoC. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00592. DeoC_type2. 1 hit.
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.
SMARTiSM01133. DeoC. 1 hit.
[Graphical view]
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)DescriptionActionsGraphical viewLength
Sequence conflicti18T → N in CAA26974 (PubMed:6749498).Curated1

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.
WP_001298497.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77334; AAC77334; b4381.
BAE78370; BAE78370; BAE78370.
GeneIDi948902.
KEGGiecj:JW4344.
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.
PIRiA01102. ADECD.
RefSeqiNP_418798.1. NC_000913.3.
WP_001298497.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JCJX-ray1.10A/B1-259[»]
1JCLX-ray1.05A/B1-259[»]
1KTNX-ray1.40A/B1-250[»]
1P1XX-ray0.99A/B1-259[»]
5EKYX-ray1.10A1-259[»]
5EL1X-ray1.25A1-259[»]
5EMUX-ray1.50A1-259[»]
ProteinModelPortaliP0A6L0.
SMRiP0A6L0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263350. 9 interactors.
IntActiP0A6L0. 8 interactors.
STRINGi511145.b4381.

2D gel databases

SWISS-2DPAGEP0A6L0.

Proteomic databases

EPDiP0A6L0.
PaxDbiP0A6L0.
PRIDEiP0A6L0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77334; AAC77334; b4381.
BAE78370; BAE78370; BAE78370.
GeneIDi948902.
KEGGiecj:JW4344.
eco:b4381.
PATRICi32124378. VBIEscCol129921_4529.

Organism-specific databases

EchoBASEiEB0217.
EcoGeneiEG10221. deoC.

Phylogenomic databases

eggNOGiENOG4105FCI. Bacteria.
COG0274. LUCA.
HOGENOMiHOG000241644.
InParanoidiP0A6L0.
KOiK01619.
OMAiKIATVTN.
PhylomeDBiP0A6L0.

Enzyme and pathway databases

UniPathwayiUPA00002; UER00468.
BioCyciEcoCyc:DEOXYRIBOSE-P-ALD-MONOMER.
ECOL316407:JW4344-MONOMER.
MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER.
BRENDAi4.1.2.4. 2026.
SABIO-RKP0A6L0.

Miscellaneous databases

EvolutionaryTraceiP0A6L0.
PROiP0A6L0.

Family and domain databases

CDDicd00959. DeoC. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00592. DeoC_type2. 1 hit.
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.
SMARTiSM01133. DeoC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00126. deoC. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 104 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.