UniProtKB - P0A6L0 (DEOC_ECOLI)
Protein
Deoxyribose-phosphate aldolase
Gene
deoC
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate (PubMed:11598300, PubMed:17905878, PubMed:6749498). Can also catalyze the double aldol condensation of three acetaldehyde molecules, leading to the formation of 2,4,6-trideoxyhexose (Ref. 5).4 Publications
Catalytic activityi
- 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphateUniRule annotation3 PublicationsEC:4.1.2.4UniRule annotation3 Publications
Kineticsi
- KM=0.23 mM for 2-deoxy-D-ribose 5-phosphate1 Publication
pH dependencei
Optimum pH is 7.5 for 2-deoxy-D-ribose 5-phosphate cleavage.1 Publication
: 2-deoxy-D-ribose 1-phosphate degradation Pathwayi
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.UniRule annotationCuratedProteins known to be involved in the 2 steps of the subpathway in this organism are:
- no protein annotated in this organism
- Deoxyribose-phosphate aldolase (deoC), Deoxyribose-phosphate aldolase (deoC)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 102 | Proton donor/acceptorUniRule annotation1 Publication | 1 | |
Active sitei | 167 | Schiff-base intermediate with acetaldehydeUniRule annotation1 Publication1 Publication | 1 | |
Active sitei | 201 | Proton donor/acceptorUniRule annotation2 Publications | 1 |
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
Keywordsi
Molecular function | Lyase |
Ligand | Schiff base |
Enzyme and pathway databases
BioCyci | EcoCyc:DEOXYRIBOSE-P-ALD-MONOMER MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER |
BRENDAi | 4.1.2.4, 2026 |
SABIO-RKi | P0A6L0 |
UniPathwayi | UPA00002;UER00468 |
Names & Taxonomyi
Protein namesi | Recommended name: Deoxyribose-phosphate aldolaseUniRule annotationCurated (EC:4.1.2.4UniRule annotation3 Publications)Short name: DERA2 PublicationsUniRule annotation Alternative name(s): 2-deoxy-D-ribose 5-phosphate aldolase1 PublicationUniRule annotationCurated PhosphodeoxyriboaldolaseUniRule annotationCurated Short name: DeoxyriboaldolaseUniRule annotationCurated |
Gene namesi | Name:deoC1 PublicationUniRule annotation Synonyms:dra, thyR Ordered Locus Names:b4381, JW4344 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotationCurated
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 47 | C → A or S: 3-fold decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 102 | D → E: 44-fold decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 102 | D → L: 2000-fold decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 102 | D → N: 1500-fold decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 137 | K → L: 20-fold decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 167 | K → L: 1000-fold decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 167 | K → R: 20-fold decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 201 | K → L: 1500-fold decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 201 | K → R: 1000-fold decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 259 | Y → F: 200-fold decrease in catalytic efficiency. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB04087, Open Form of 2'-Deoxy-Ribofuranose-5'-Phosphate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000057296 | 1 – 259 | Deoxyribose-phosphate aldolaseAdd BLAST | 259 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 167 | N6-acetyllysine1 Publication | 1 |
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P0A6L0 |
PaxDbi | P0A6L0 |
PRIDEi | P0A6L0 |
2D gel databases
SWISS-2DPAGEi | P0A6L0 |
PTM databases
iPTMneti | P0A6L0 |
Interactioni
Subunit structurei
Monomer and homodimer.
2 PublicationsProtein-protein interaction databases
BioGRIDi | 4263350, 25 interactors |
IntActi | P0A6L0, 8 interactors |
STRINGi | 511145.b4381 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A6L0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A6L0 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0274, Bacteria |
HOGENOMi | CLU_053595_3_1_6 |
InParanoidi | P0A6L0 |
PhylomeDBi | P0A6L0 |
Family and domain databases
CDDi | cd00959, DeoC, 1 hit |
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_00592, DeoC_type2, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR011343, DeoC IPR002915, DeoC/FbaB/LacD_aldolase IPR023649, DeoC_typeII |
PANTHERi | PTHR10889, PTHR10889, 1 hit |
Pfami | View protein in Pfam PF01791, DeoC, 1 hit |
PIRSFi | PIRSF001357, DeoC, 1 hit |
SMARTi | View protein in SMART SM01133, DeoC, 1 hit |
TIGRFAMsi | TIGR00126, deoC, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A6L0-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 18 | T → N in CAA26974 (PubMed:6749498).Curated | 1 |
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 WP_001298497.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC77334; AAC77334; b4381 BAE78370; BAE78370; BAE78370 |
GeneIDi | 948902 |
KEGGi | ecj:JW4344 eco:b4381 |
PATRICi | fig|1411691.4.peg.2304 |
Similar proteinsi
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 WP_001298497.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
5EKY | X-ray | 1.10 | A | 1-259 | [»] | |
5EL1 | X-ray | 1.25 | A | 1-259 | [»] | |
5EMU | X-ray | 1.50 | A | 1-259 | [»] | |
SMRi | P0A6L0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263350, 25 interactors |
IntActi | P0A6L0, 8 interactors |
STRINGi | 511145.b4381 |
Chemistry databases
DrugBanki | DB04087, Open Form of 2'-Deoxy-Ribofuranose-5'-Phosphate |
PTM databases
iPTMneti | P0A6L0 |
2D gel databases
SWISS-2DPAGEi | P0A6L0 |
Proteomic databases
jPOSTi | P0A6L0 |
PaxDbi | P0A6L0 |
PRIDEi | P0A6L0 |
Genome annotation databases
EnsemblBacteriai | AAC77334; AAC77334; b4381 BAE78370; BAE78370; BAE78370 |
GeneIDi | 948902 |
KEGGi | ecj:JW4344 eco:b4381 |
PATRICi | fig|1411691.4.peg.2304 |
Organism-specific databases
EchoBASEi | EB0217 |
Phylogenomic databases
eggNOGi | COG0274, Bacteria |
HOGENOMi | CLU_053595_3_1_6 |
InParanoidi | P0A6L0 |
PhylomeDBi | P0A6L0 |
Enzyme and pathway databases
UniPathwayi | UPA00002;UER00468 |
BioCyci | EcoCyc:DEOXYRIBOSE-P-ALD-MONOMER MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER |
BRENDAi | 4.1.2.4, 2026 |
SABIO-RKi | P0A6L0 |
Miscellaneous databases
EvolutionaryTracei | P0A6L0 |
PROi | PR:P0A6L0 |
Family and domain databases
CDDi | cd00959, DeoC, 1 hit |
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_00592, DeoC_type2, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR011343, DeoC IPR002915, DeoC/FbaB/LacD_aldolase IPR023649, DeoC_typeII |
PANTHERi | PTHR10889, PTHR10889, 1 hit |
Pfami | View protein in Pfam PF01791, DeoC, 1 hit |
PIRSFi | PIRSF001357, DeoC, 1 hit |
SMARTi | View protein in SMART SM01133, DeoC, 1 hit |
TIGRFAMsi | TIGR00126, deoC, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DEOC_ECOLI | |
Accessioni | P0A6L0Primary (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: | April 7, 2021 | |
This is version 129 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- 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