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Protein

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC

Gene

kdsC

Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of lipopolysaccharides (LPSs) (By similarity). Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate.By similarity1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication

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

This protein is involved in step 3 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi32Magnesium1
Metal bindingi34Magnesium; via carbonyl oxygen1
Binding sitei34Substrate1 Publication1
Binding sitei63Substrate1 Publication1
Binding sitei78Substrate1 Publication1
Binding sitei86Substrate1 Publication1
Binding sitei102Substrate1 Publication1
Metal bindingi125Magnesium1
Binding sitei187Substrate; via carbonyl oxygen1 Publication1

GO - Molecular functioni

  • 3-deoxy-manno-octulosonate-8-phosphatase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • lipopolysaccharide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciECOL199310:C3958-MONOMER.
UniPathwayiUPA00030.
UPA00357; UER00475.

Names & Taxonomyi

Protein namesi
Recommended name:
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC (EC:3.1.3.45)
Alternative name(s):
KDO 8-P phosphatase
Gene namesi
Name:kdsC
Ordered Locus Names:c3958
OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic identifieri199310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000001410 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002016981 – 1883-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsCAdd BLAST188

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi199310.c3958.

Structurei

Secondary structure

1188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 24Combined sources8
Beta strandi27 – 31Combined sources5
Helixi33 – 37Combined sources5
Beta strandi40 – 45Combined sources6
Beta strandi50 – 55Combined sources6
Helixi56 – 66Combined sources11
Turni67 – 69Combined sources3
Beta strandi71 – 75Combined sources5
Helixi81 – 90Combined sources10
Beta strandi94 – 96Combined sources3
Helixi103 – 113Combined sources11
Helixi117 – 119Combined sources3
Beta strandi120 – 126Combined sources7
Helixi127 – 129Combined sources3
Helixi130 – 133Combined sources4
Beta strandi136 – 141Combined sources6
Turni147 – 149Combined sources3
Helixi150 – 152Combined sources3
Beta strandi153 – 156Combined sources4
Turni161 – 164Combined sources4
Helixi165 – 176Combined sources12
Turni180 – 182Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R8EX-ray1.40A/B/C/D/E/F/G/H1-188[»]
2R8XX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-188[»]
2R8YX-ray1.85A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-188[»]
2R8ZX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-188[»]
3HYCX-ray3.06A/B/C/D/E/F/G/H1-188[»]
3I6BX-ray2.49A/B/C/D1-180[»]
ProteinModelPortaliP67653.
SMRiP67653.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP67653.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 34Substrate binding3
Regioni55 – 59Substrate binding5
Regioni76 – 77Substrate binding2

Sequence similaritiesi

Belongs to the KdsC family.Curated

Phylogenomic databases

eggNOGiENOG4108Z4R. Bacteria.
COG1778. LUCA.
HOGENOMiHOG000264740.
KOiK03270.
OMAiFDENFHE.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR010023. KDO_8-P_phosphatase.
[Graphical view]
PfamiPF08282. Hydrolase_3. 1 hit.
[Graphical view]
PIRSFiPIRSF006118. KDO8-P_Ptase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01670. KdsC-phosphatas. 1 hit.

Sequencei

Sequence statusi: Complete.

P67653-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKAGASLAT CYGPVSADVM AKAENIRLLI LDVDGVLSDG LIYMGNNGEE
60 70 80 90 100
LKAFNVRDGY GIRCALTSDI EVAIITGRKA KLVEDRCATL GITHLYQGQS
110 120 130 140 150
NKLIAFSDLL EKLAIAPENV AYVGDDLIDW PVMEKVGLSV AVADAHPLLI
160 170 180
PRADYVTRIA GGRGAVREVC DLLLLAQGKL DEAKGQSI
Length:188
Mass (Da):20,015
Last modified:October 11, 2004 - v1
Checksum:i6A40ED8C20B1E3A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN82398.1.
RefSeqiWP_000030016.1. NC_004431.1.

Genome annotation databases

EnsemblBacteriaiAAN82398; AAN82398; c3958.
KEGGiecc:c3958.
PATRICi18285690. VBIEscCol75197_3725.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN82398.1.
RefSeqiWP_000030016.1. NC_004431.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R8EX-ray1.40A/B/C/D/E/F/G/H1-188[»]
2R8XX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-188[»]
2R8YX-ray1.85A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-188[»]
2R8ZX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-188[»]
3HYCX-ray3.06A/B/C/D/E/F/G/H1-188[»]
3I6BX-ray2.49A/B/C/D1-180[»]
ProteinModelPortaliP67653.
SMRiP67653.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi199310.c3958.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN82398; AAN82398; c3958.
KEGGiecc:c3958.
PATRICi18285690. VBIEscCol75197_3725.

Phylogenomic databases

eggNOGiENOG4108Z4R. Bacteria.
COG1778. LUCA.
HOGENOMiHOG000264740.
KOiK03270.
OMAiFDENFHE.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00357; UER00475.
BioCyciECOL199310:C3958-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP67653.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR010023. KDO_8-P_phosphatase.
[Graphical view]
PfamiPF08282. Hydrolase_3. 1 hit.
[Graphical view]
PIRSFiPIRSF006118. KDO8-P_Ptase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01670. KdsC-phosphatas. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKDSC_ECOL6
AccessioniPrimary (citable) accession number: P67653
Secondary accession number(s): Q83JF3, Q8FD72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 81 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.