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Protein

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

Gene

kdsC

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

Functioni

Involved in the biosynthesis of lipopolysaccharides (LPSs), but is not essential (PubMed:16765569). Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate (PubMed:12639950, PubMed:16765569).2 Publications

Catalytic activityi

3-deoxy-D-manno-octulosonate 8-phosphate + H2O = 3-deoxy-D-manno-octulosonate + phosphate.1 Publication

Cofactori

Mg2+1 Publication, Co2+1 PublicationNote: Mg2+. The phosphatase activity is also stimulated by cobalt ions, whereas baryum, zinc, and manganese ions are less effective stimulators.1 Publication

Enzyme regulationi

Inhibited by calcium, cadmium, mercury, and copper ions.1 Publication

pH dependencei

Optimum pH is 5.5 (at pH 7.5 and 37 degrees Celsius).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 bindingi32MagnesiumBy similarity1
Metal bindingi34Magnesium; via carbonyl oxygenBy similarity1
Binding sitei34SubstrateBy similarity1
Binding sitei63SubstrateBy similarity1
Binding sitei78SubstrateBy similarity1
Binding sitei86SubstrateBy similarity1
Binding sitei102SubstrateBy similarity1
Metal bindingi125MagnesiumBy similarity1
Binding sitei187Substrate; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • lipopolysaccharide biosynthetic process Source: UniProtKB

Keywordsi

Molecular functionHydrolase
Biological processLipopolysaccharide biosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7663-MONOMER
UniPathwayiUPA00030
UPA00357; UER00475

Names & Taxonomyi

Protein namesi
Recommended name:
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC (EC:3.1.3.451 Publication)
Alternative name(s):
KDO 8-P phosphatase
Gene namesi
Name:kdsC
Synonyms:yrbI, yrbJ
Ordered Locus Names:b3198, JW3165
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12804 kdsC

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002016962 – 1883-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsCAdd BLAST187

Proteomic databases

PaxDbiP0ABZ4
PRIDEiP0ABZ4

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi4261882, 248 interactors
DIPiDIP-48034N
IntActiP0ABZ4, 2 interactors
STRINGi316385.ECDH10B_3372

Structurei

3D structure databases

ProteinModelPortaliP0ABZ4
SMRiP0ABZ4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 34Substrate bindingBy similarity3
Regioni55 – 59Substrate bindingBy similarity5
Regioni76 – 77Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the KdsC family.Curated

Phylogenomic databases

eggNOGiENOG4108Z4R Bacteria
COG1778 LUCA
HOGENOMiHOG000264740
InParanoidiP0ABZ4
KOiK03270
OMAiCVGDDYN
PhylomeDBiP0ABZ4

Family and domain databases

Gene3Di3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR010023 KdsC_fam
PIRSFiPIRSF006118 KDO8-P_Ptase, 1 hit
SFLDiSFLDG01138 C1.6.2:_Deoxy-d-mannose-octulo, 1 hit
SUPFAMiSSF56784 SSF56784, 1 hit
TIGRFAMsiTIGR01670 KdsC-phosphatas, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ABZ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKAGASLAT CYGPVSADVI 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):19,997
Last modified:November 8, 2005 - v1
Checksum:i75AF512CF4E5E6E2
GO

Sequence cautioni

The sequence AAA57999 differs from that shown. Reason: Frameshift at position 116.Curated
The sequence AAA58000 differs from that shown. Reason: Frameshift at position 116.Curated
The sequence AAA58000 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Mass spectrometryi

Molecular mass is 19881 Da from positions 2 - 188. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA Translation: AAA57999.1 Frameshift.
U18997 Genomic DNA Translation: AAA58000.1 Sequence problems.
U00096 Genomic DNA Translation: AAC76230.1
AP009048 Genomic DNA Translation: BAE77242.1
PIRiH65110
RefSeqiNP_417665.1, NC_000913.3
WP_000030005.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76230; AAC76230; b3198
BAE77242; BAE77242; BAE77242
GeneIDi947717
KEGGiecj:JW3165
eco:b3198
PATRICifig|1411691.4.peg.3533

Similar proteinsi

Entry informationi

Entry nameiKDSC_ECOLI
AccessioniPrimary (citable) accession number: P0ABZ4
Secondary accession number(s): P45396, P45398, Q2M914
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: May 23, 2018
This is version 102 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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. SIMILARITY comments
    Index of protein domains and families

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