UniProtKB - P0A715 (KDSA_ECOLI)
Protein
2-dehydro-3-deoxyphosphooctonate aldolase
Gene
kdsA
Organism
Escherichia coli (strain K12)
Status
Functioni
Synthesis of KDO 8-P which is required for lipid A maturation and cellular growth.
Catalytic activityi
- D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-α-D-manno-2-octulosonate-8-phosphate + phosphateEC:2.5.1.55
: 3-deoxy-D-manno-octulosonate biosynthesis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate.Proteins known to be involved in the 3 steps of the subpathway in this organism are:
- Arabinose 5-phosphate isomerase KdsD (kdsD)
- 2-dehydro-3-deoxyphosphooctonate aldolase (kdsA), 2-dehydro-3-deoxyphosphooctonate aldolase (kdsA)
- 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC (kdsC), 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC (kdsC)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate, the pathway 3-deoxy-D-manno-octulosonate biosynthesis and in Carbohydrate biosynthesis.
Pathwayi: lipopolysaccharide biosynthesis
This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.
GO - Molecular functioni
- 3-deoxy-8-phosphooctulonate synthase activity Source: EcoCyc
- identical protein binding Source: EcoCyc
GO - Biological processi
- keto-3-deoxy-D-manno-octulosonic acid biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Transferase |
Biological process | Lipopolysaccharide biosynthesis |
Enzyme and pathway databases
BioCyci | EcoCyc:KDO-8PSYNTH-MONOMER MetaCyc:KDO-8PSYNTH-MONOMER |
BRENDAi | 2.5.1.55, 2026 |
SABIO-RKi | P0A715 |
UniPathwayi | UPA00030 UPA00357;UER00474 |
Names & Taxonomyi
Protein namesi | Recommended name: 2-dehydro-3-deoxyphosphooctonate aldolase (EC:2.5.1.55)Alternative name(s): 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase KDO-8-phosphate synthase Short name: KDO 8-P synthase Short name: KDOPS Phospho-2-dehydro-3-deoxyoctonate aldolase |
Gene namesi | Name:kdsA Ordered Locus Names:b1215, JW1206 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
Cytosol
- cytosol Source: EcoCyc
Other locations
- protein-containing complex Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000187124 | 1 – 284 | 2-dehydro-3-deoxyphosphooctonate aldolaseAdd BLAST | 284 |
Proteomic databases
jPOSTi | P0A715 |
PaxDbi | P0A715 |
PRIDEi | P0A715 |
2D gel databases
SWISS-2DPAGEi | P0A715 |
Interactioni
Subunit structurei
Homotrimer.
GO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4260117, 448 interactors |
DIPi | DIP-35940N |
IntActi | P0A715, 47 interactors |
STRINGi | 511145.b1215 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A715 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A715 |
Family & Domainsi
Sequence similaritiesi
Belongs to the KdsA family.Curated
Phylogenomic databases
eggNOGi | COG2877, Bacteria |
HOGENOMi | CLU_036666_0_0_6 |
InParanoidi | P0A715 |
PhylomeDBi | P0A715 |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_00056, KDO8P_synth, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR006218, DAHP1/KDSA IPR006269, KDO8P_synthase |
PANTHERi | PTHR21057, PTHR21057, 1 hit |
Pfami | View protein in Pfam PF00793, DAHP_synth_1, 1 hit |
TIGRFAMsi | TIGR01362, KDO8P_synth, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A715-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKQKVVSIGD INVANDLPFV LFGGMNVLES RDLAMRICEH YVTVTQKLGI
60 70 80 90 100
PYVFKASFDK ANRSSIHSYR GPGLEEGMKI FQELKQTFGV KIITDVHEPS
110 120 130 140 150
QAQPVADVVD VIQLPAFLAR QTDLVEAMAK TGAVINVKKP QFVSPGQMGN
160 170 180 190 200
IVDKFKEGGN EKVILCDRGA NFGYDNLVVD MLGFSIMKKV SGNSPVIFDV
210 220 230 240 250
THALQCRDPF GAASGGRRAQ VAELARAGMA VGLAGLFIEA HPDPEHAKCD
260 270 280
GPSALPLAKL EPFLKQMKAI DDLVKGFEEL DTSK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 22 | F → L in CAA29067 (PubMed:3039295).Curated | 1 |
Mass spectrometryi
Molecular mass is 30842±17 Da. Determined by ESI. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X05552 Genomic DNA Translation: CAA29067.1 U18555 Genomic DNA Translation: AAC43441.1 U00096 Genomic DNA Translation: AAC74299.1 AP009048 Genomic DNA Translation: BAA36073.1 |
PIRi | I83573, SYECOL |
RefSeqi | NP_415733.1, NC_000913.3 WP_000811065.1, NZ_STEB01000023.1 |
Genome annotation databases
EnsemblBacteriai | AAC74299; AAC74299; b1215 BAA36073; BAA36073; BAA36073 |
GeneIDi | 58460426 945785 |
KEGGi | ecj:JW1206 eco:b1215 |
PATRICi | fig|1411691.4.peg.1069 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X05552 Genomic DNA Translation: CAA29067.1 U18555 Genomic DNA Translation: AAC43441.1 U00096 Genomic DNA Translation: AAC74299.1 AP009048 Genomic DNA Translation: BAA36073.1 |
PIRi | I83573, SYECOL |
RefSeqi | NP_415733.1, NC_000913.3 WP_000811065.1, NZ_STEB01000023.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1D9E | X-ray | 2.40 | A/B/C/D | 1-284 | [»] | |
1G7U | X-ray | 2.80 | A | 1-284 | [»] | |
1G7V | X-ray | 2.40 | A | 1-284 | [»] | |
1GG0 | X-ray | 3.00 | A | 1-284 | [»] | |
1PHQ | X-ray | 2.70 | A | 1-284 | [»] | |
1PHW | X-ray | 2.36 | A | 1-284 | [»] | |
1PL9 | X-ray | 2.90 | A | 1-284 | [»] | |
1Q3N | X-ray | 2.70 | A | 1-284 | [»] | |
1X6U | X-ray | 2.70 | A | 1-284 | [»] | |
1X8F | X-ray | 2.40 | A | 1-284 | [»] | |
6U57 | X-ray | 2.80 | A | 1-284 | [»] | |
SMRi | P0A715 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260117, 448 interactors |
DIPi | DIP-35940N |
IntActi | P0A715, 47 interactors |
STRINGi | 511145.b1215 |
2D gel databases
SWISS-2DPAGEi | P0A715 |
Proteomic databases
jPOSTi | P0A715 |
PaxDbi | P0A715 |
PRIDEi | P0A715 |
Genome annotation databases
EnsemblBacteriai | AAC74299; AAC74299; b1215 BAA36073; BAA36073; BAA36073 |
GeneIDi | 58460426 945785 |
KEGGi | ecj:JW1206 eco:b1215 |
PATRICi | fig|1411691.4.peg.1069 |
Organism-specific databases
EchoBASEi | EB0513 |
Phylogenomic databases
eggNOGi | COG2877, Bacteria |
HOGENOMi | CLU_036666_0_0_6 |
InParanoidi | P0A715 |
PhylomeDBi | P0A715 |
Enzyme and pathway databases
UniPathwayi | UPA00030 UPA00357;UER00474 |
BioCyci | EcoCyc:KDO-8PSYNTH-MONOMER MetaCyc:KDO-8PSYNTH-MONOMER |
BRENDAi | 2.5.1.55, 2026 |
SABIO-RKi | P0A715 |
Miscellaneous databases
EvolutionaryTracei | P0A715 |
PROi | PR:P0A715 |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_00056, KDO8P_synth, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR006218, DAHP1/KDSA IPR006269, KDO8P_synthase |
PANTHERi | PTHR21057, PTHR21057, 1 hit |
Pfami | View protein in Pfam PF00793, DAHP_synth_1, 1 hit |
TIGRFAMsi | TIGR01362, KDO8P_synth, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | KDSA_ECOLI | |
Accessioni | P0A715Primary (citable) accession number: P0A715 Secondary accession number(s): P17579 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 7, 2005 |
Last sequence update: | June 7, 2005 | |
Last modified: | April 7, 2021 | |
This is version 128 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