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P0A715

- KDSA_ECOLI

UniProt

P0A715 - KDSA_ECOLI

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Protein

2-dehydro-3-deoxyphosphooctonate aldolase

Gene

kdsA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 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 = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate.

Pathwayi

GO - Molecular functioni

  1. 3-deoxy-8-phosphooctulonate synthase activity Source: EcoCyc

GO - Biological processi

  1. keto-3-deoxy-D-manno-octulosonic acid biosynthetic process Source: UniProtKB-HAMAP
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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10518. kdsA.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2842842-dehydro-3-deoxyphosphooctonate aldolasePRO_0000187124Add
BLAST

Proteomic databases

PaxDbiP0A715.
PRIDEiP0A715.

2D gel databases

SWISS-2DPAGEP0A715.

Expressioni

Gene expression databases

GenevestigatoriP0A715.

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

DIPiDIP-35940N.
IntActiP0A715. 46 interactions.
MINTiMINT-1220797.
STRINGi511145.b1215.

Structurei

Secondary structure

1
284
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83
Beta strandi11 – 133
Beta strandi15 – 173
Beta strandi20 – 223
Beta strandi24 – 274
Helixi31 – 4818
Beta strandi55 – 584
Beta strandi64 – 685
Helixi74 – 8815
Beta strandi93 – 953
Turni99 – 1013
Helixi102 – 1087
Beta strandi110 – 1145
Helixi116 – 1194
Helixi122 – 13110
Beta strandi134 – 1396
Helixi145 – 1473
Helixi148 – 1569
Turni157 – 1593
Beta strandi163 – 1675
Beta strandi173 – 1753
Helixi183 – 1908
Turni191 – 1933
Beta strandi196 – 1994
Helixi201 – 2044
Beta strandi211 – 2133
Turni219 – 2224
Helixi223 – 2319
Beta strandi234 – 2374
Beta strandi240 – 2423
Helixi244 – 2474
Beta strandi250 – 2523
Helixi257 – 2593
Helixi260 – 27516

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 1-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A715.

Family & Domainsi

Sequence similaritiesi

Belongs to the KdsA family.Curated

Phylogenomic databases

eggNOGiCOG2877.
HOGENOMiHOG000023021.
InParanoidiP0A715.
KOiK01627.
OMAiANDKPMV.
OrthoDBiEOG680X4R.
PhylomeDBiP0A715.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00056. KDO8P_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006269. KDO8P_synthase.
[Graphical view]
PANTHERiPTHR21057:SF2. PTHR21057:SF2. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221F → L in CAA29067. (PubMed:3039295)Curated

Mass spectrometryi

Molecular mass is 30842±17 Da from positions 1 - 284. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_489482.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74299; AAC74299; b1215.
BAA36073; BAA36073; BAA36073.
GeneIDi12931123.
945785.
KEGGiecj:Y75_p1187.
eco:b1215.
PATRICi32117682. VBIEscCol129921_1263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_489482.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P0A715.
SMRi P0A715. Positions 1-284.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35940N.
IntActi P0A715. 46 interactions.
MINTi MINT-1220797.
STRINGi 511145.b1215.

2D gel databases

SWISS-2DPAGE P0A715.

Proteomic databases

PaxDbi P0A715.
PRIDEi P0A715.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74299 ; AAC74299 ; b1215 .
BAA36073 ; BAA36073 ; BAA36073 .
GeneIDi 12931123.
945785.
KEGGi ecj:Y75_p1187.
eco:b1215.
PATRICi 32117682. VBIEscCol129921_1263.

Organism-specific databases

EchoBASEi EB0513.
EcoGenei EG10518. kdsA.

Phylogenomic databases

eggNOGi COG2877.
HOGENOMi HOG000023021.
InParanoidi P0A715.
KOi K01627.
OMAi ANDKPMV.
OrthoDBi EOG680X4R.
PhylomeDBi P0A715.

Enzyme and pathway databases

UniPathwayi UPA00030 .
UPA00357 ; UER00474 .
BioCyci EcoCyc:KDO-8PSYNTH-MONOMER.
ECOL316407:JW1206-MONOMER.
MetaCyc:KDO-8PSYNTH-MONOMER.
SABIO-RK P0A715.

Miscellaneous databases

EvolutionaryTracei P0A715.
PROi P0A715.

Gene expression databases

Genevestigatori P0A715.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00056. KDO8P_synth.
InterProi IPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006269. KDO8P_synthase.
[Graphical view ]
PANTHERi PTHR21057:SF2. PTHR21057:SF2. 1 hit.
Pfami PF00793. DAHP_synth_1. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01362. KDO8P_synth. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The kdsA gene coding for 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase is part of an operon in Escherichia coli."
    Woisetschlaeger M., Hoegenauer G.
    Mol. Gen. Genet. 207:369-373(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12."
    Strohmaier H., Remler P., Renner W., Hoegenauer G.
    J. Bacteriol. 177:4488-4500(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  7. "Overproduction and one-step purification of Escherichia coli 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase and oxygen transfer studies during catalysis using isotopic-shifted heteronuclear NMR."
    Dotson G.D., Dua R.K., Clemens J.C., Wooten E.W., Woodard R.W.
    J. Biol. Chem. 270:13698-13705(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 1-10.
  8. "3-deoxy-D-manno-octulosonate-8-phosphate synthase from Escherichia coli. Model of binding of phosphoenolpyruvate and D-arabinose-5-phosphate."
    Wagner T., Kretsinger R.H., Bauerle R., Tolbert W.D.
    J. Mol. Biol. 301:233-238(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  9. "Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor."
    Asojo O., Friedman J., Adir N., Belakhov V., Shoham Y., Baasov T.
    Biochemistry 40:6326-6334(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MASS SPECTROMETRY.

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: October 29, 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, 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

External Data

Dasty 3