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Protein

2-dehydro-3-deoxyphosphooctonate aldolase

Gene

kdsA

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

Functioni

Synthesis of KDO 8-P which is required for lipid A maturation and cellular growth.

Catalytic activityi

Phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate.

Pathwayi: 3-deoxy-D-manno-octulosonate biosynthesis

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:
  1. Arabinose 5-phosphate isomerase KdsD (kdsD)
  2. 2-dehydro-3-deoxyphosphooctonate aldolase (kdsA)
  3. 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC (kdsC)
This subpathway is part of the pathway 3-deoxy-D-manno-octulosonate biosynthesis, which is itself part of Carbohydrate biosynthesis.
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

GO - Biological processi

  • keto-3-deoxy-D-manno-octulosonic acid biosynthetic process Source: EcoCyc
  • protein homotetramerization Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:KDO-8PSYNTH-MONOMER.
ECOL316407:JW1206-MONOMER.
MetaCyc:KDO-8PSYNTH-MONOMER.
BRENDAi2.5.1.55. 2026.
SABIO-RKP0A715.
UniPathwayiUPA00030.
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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10518. kdsA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001871241 – 2842-dehydro-3-deoxyphosphooctonate aldolaseAdd BLAST284

Proteomic databases

EPDiP0A715.
PaxDbiP0A715.
PRIDEiP0A715.

2D gel databases

SWISS-2DPAGEP0A715.

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

BioGridi4260117. 422 interactors.
DIPiDIP-35940N.
IntActiP0A715. 46 interactors.
MINTiMINT-1220797.
STRINGi511145.b1215.

Structurei

Secondary structure

1284
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Beta strandi11 – 13Combined sources3
Beta strandi15 – 17Combined sources3
Beta strandi20 – 22Combined sources3
Beta strandi24 – 27Combined sources4
Helixi31 – 48Combined sources18
Beta strandi55 – 58Combined sources4
Beta strandi64 – 68Combined sources5
Helixi74 – 88Combined sources15
Beta strandi93 – 95Combined sources3
Turni99 – 101Combined sources3
Helixi102 – 108Combined sources7
Beta strandi110 – 114Combined sources5
Helixi116 – 119Combined sources4
Helixi122 – 131Combined sources10
Beta strandi134 – 139Combined sources6
Helixi145 – 147Combined sources3
Helixi148 – 156Combined sources9
Turni157 – 159Combined sources3
Beta strandi163 – 167Combined sources5
Beta strandi173 – 175Combined sources3
Helixi183 – 190Combined sources8
Turni191 – 193Combined sources3
Beta strandi196 – 199Combined sources4
Helixi201 – 204Combined sources4
Beta strandi211 – 213Combined sources3
Turni219 – 222Combined sources4
Helixi223 – 231Combined sources9
Beta strandi234 – 237Combined sources4
Beta strandi240 – 242Combined sources3
Helixi244 – 247Combined sources4
Beta strandi250 – 252Combined sources3
Helixi257 – 259Combined sources3
Helixi260 – 275Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D9EX-ray2.40A/B/C/D1-284[»]
1G7UX-ray2.80A1-284[»]
1G7VX-ray2.40A1-284[»]
1GG0X-ray3.00A1-284[»]
1PHQX-ray2.70A1-284[»]
1PHWX-ray2.36A1-284[»]
1PL9X-ray2.90A1-284[»]
1Q3NX-ray2.70A1-284[»]
1X6UX-ray2.70A1-284[»]
1X8FX-ray2.40A1-284[»]
ProteinModelPortaliP0A715.
SMRiP0A715.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A715.

Family & Domainsi

Sequence similaritiesi

Belongs to the KdsA family.Curated

Phylogenomic databases

eggNOGiENOG4105CXR. Bacteria.
COG2877. LUCA.
HOGENOMiHOG000023021.
InParanoidiP0A715.
KOiK01627.
OMAiFRGIPTM.
PhylomeDBiP0A715.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00056. KDO8P_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006269. KDO8P_synthase.
[Graphical view]
PfamiPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01362. KDO8P_synth. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A715-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:284
Mass (Da):30,833
Last modified:June 7, 2005 - v1
Checksum:i35E79D692D134535
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22F → L in CAA29067 (PubMed:3039295).Curated1

Mass spectrometryi

Molecular mass is 30842±17 Da from positions 1 - 284. 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.
PIRiI83573. SYECOL.
RefSeqiNP_415733.1. NC_000913.3.
WP_000811065.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74299; AAC74299; b1215.
BAA36073; BAA36073; BAA36073.
GeneIDi945785.
KEGGiecj:JW1206.
eco:b1215.
PATRICi32117682. VBIEscCol129921_1263.

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.
PIRiI83573. SYECOL.
RefSeqiNP_415733.1. NC_000913.3.
WP_000811065.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D9EX-ray2.40A/B/C/D1-284[»]
1G7UX-ray2.80A1-284[»]
1G7VX-ray2.40A1-284[»]
1GG0X-ray3.00A1-284[»]
1PHQX-ray2.70A1-284[»]
1PHWX-ray2.36A1-284[»]
1PL9X-ray2.90A1-284[»]
1Q3NX-ray2.70A1-284[»]
1X6UX-ray2.70A1-284[»]
1X8FX-ray2.40A1-284[»]
ProteinModelPortaliP0A715.
SMRiP0A715.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260117. 422 interactors.
DIPiDIP-35940N.
IntActiP0A715. 46 interactors.
MINTiMINT-1220797.
STRINGi511145.b1215.

2D gel databases

SWISS-2DPAGEP0A715.

Proteomic databases

EPDiP0A715.
PaxDbiP0A715.
PRIDEiP0A715.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74299; AAC74299; b1215.
BAA36073; BAA36073; BAA36073.
GeneIDi945785.
KEGGiecj:JW1206.
eco:b1215.
PATRICi32117682. VBIEscCol129921_1263.

Organism-specific databases

EchoBASEiEB0513.
EcoGeneiEG10518. kdsA.

Phylogenomic databases

eggNOGiENOG4105CXR. Bacteria.
COG2877. LUCA.
HOGENOMiHOG000023021.
InParanoidiP0A715.
KOiK01627.
OMAiFRGIPTM.
PhylomeDBiP0A715.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00357; UER00474.
BioCyciEcoCyc:KDO-8PSYNTH-MONOMER.
ECOL316407:JW1206-MONOMER.
MetaCyc:KDO-8PSYNTH-MONOMER.
BRENDAi2.5.1.55. 2026.
SABIO-RKP0A715.

Miscellaneous databases

EvolutionaryTraceiP0A715.
PROiP0A715.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00056. KDO8P_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006269. KDO8P_synthase.
[Graphical view]
PfamiPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01362. KDO8P_synth. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKDSA_ECOLI
AccessioniPrimary (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: November 2, 2016
This is version 102 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, Direct protein sequencing, 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.