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Q8ZLS0 (KDSC_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC

EC=3.1.3.45
Alternative name(s):
KDO 8-P phosphatase
Gene names
Name:kdsC
Ordered Locus Names:STM3316
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the biosynthesis of lipopolysaccharides (LPSs). 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 similarity.

Catalytic activity

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

Cofactor

Magnesium Probable.

Pathway

Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3.

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the kdsC family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1881883-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC
PRO_0000201700

Regions

Region32 – 343Substrate binding By similarity
Region55 – 595Substrate binding By similarity
Region76 – 772Substrate binding By similarity

Sites

Metal binding321Magnesium By similarity
Metal binding341Magnesium; via carbonyl oxygen By similarity
Metal binding1251Magnesium By similarity
Binding site341Substrate By similarity
Binding site631Substrate By similarity
Binding site781Substrate By similarity
Binding site861Substrate By similarity
Binding site1021Substrate By similarity
Binding site1871Substrate; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZLS0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: DC28AB5DD2034F97

FASTA18820,071
        10         20         30         40         50         60 
MSKAGASLAT CYGPVSPHVM TKAENIRLLI LDVDGVLSDG LIYMGNNGEE LKAFNVRDGY 

        70         80         90        100        110        120 
GIRCALTSNI EVAIITGRKA KLVEDRCATL GIVHLYQGQS NKLIAFSDLL EKLAIAPENV 

       130        140        150        160        170        180 
AYVGDDLIDW PVMEKVGLSV AVADAHPLLI PRADYVTHIA GGRGAVREVC DLLLLAQGKL 


DEAKGQSI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL22185.1.
RefSeqNP_462226.1. NC_003197.1.

3D structure databases

ProteinModelPortalQ8ZLS0.
ModBaseSearch...

Proteomic databases

PRIDEQ8ZLS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1254839.
GenomeReviewsGene locus STM3316 in contig AE006468_GR.
KEGGstm:STM3316.
NMPDRfig|99287.1.peg.3202.
PATRIC32385427. VBISalEnt20916_3517.

Phylogenomic databases

HOGENOMHBG471796.
OMAKTFNTLD.
ProtClustDBPRK09484.

Enzyme and pathway databases

BioCycSTYP99287:STM3316-MONOMER.

Family and domain databases

InterProIPR023214. HAD-like_dom.
IPR013200. HAD-SF_hydro-like_3.
IPR010023. KDO_8-P_phosphatase.
[Graphical view]
Gene3DG3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KOK03270.
PANTHERPTHR26053. PTHR26053. 1 hit.
PfamPF08282. Hydrolase_3. 1 hit.
[Graphical view]
PIRSFPIRSF006118. KDO8-P_Ptase. 1 hit.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01670. YrbI-phosphatas. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKDSC_SALTY
AccessionPrimary (citable) accession number: Q8ZLS0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families