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Protein

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

Gene

HI_1679

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of lipopolysaccharides (LPSs), but is not essential. Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate.1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi14MagnesiumCurated1
Metal bindingi16MagnesiumCurated1
Binding sitei16SubstrateBy similarity1
Binding sitei60SubstrateBy similarity1
Binding sitei68SubstrateBy similarity1
Binding sitei84SubstrateBy similarity1
Metal bindingi107MagnesiumCurated1
Binding sitei174Substrate; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

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
Ordered Locus Names:HI_1679
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002017031 – 1803-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsCAdd BLAST180

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi71421.HI1679.

Structurei

Secondary structure

1180
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Beta strandi10 – 14Combined sources5
Turni16 – 18Combined sources3
Beta strandi22 – 27Combined sources6
Beta strandi30 – 37Combined sources8
Helixi38 – 49Combined sources12
Beta strandi53 – 59Combined sources7
Helixi63 – 72Combined sources10
Beta strandi76 – 80Combined sources5
Helixi84 – 95Combined sources12
Helixi99 – 101Combined sources3
Beta strandi102 – 106Combined sources5
Helixi109 – 111Combined sources3
Helixi112 – 117Combined sources6
Beta strandi118 – 123Combined sources6
Helixi129 – 132Combined sources4
Beta strandi135 – 138Combined sources4
Turni143 – 146Combined sources4
Helixi147 – 158Combined sources12
Helixi163 – 166Combined sources4
Helixi168 – 174Combined sources7
Helixi175 – 177Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J8DX-ray2.30A/B/C/D1-180[»]
1K1EX-ray1.67A/B/C/D/E/F/G/H/I/J/K/L1-180[»]
4HGPX-ray1.80A1-180[»]
ProteinModelPortaliP45314.
SMRiP45314.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45314.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 16Substrate bindingBy similarity3
Regioni37 – 41Substrate bindingBy similarity5
Regioni58 – 59Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the KdsC family.Curated

Phylogenomic databases

eggNOGiENOG4108Z4R. Bacteria.
COG1778. LUCA.
KOiK03270.
OMAiFDENFHE.
PhylomeDBiP45314.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR010023. KDO_8-P_phosphatase.
[Graphical view]
PfamiPF08282. Hydrolase_3. 1 hit.
[Graphical view]
PIRSFiPIRSF006118. KDO8-P_Ptase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01670. KdsC-phosphatas. 1 hit.

Sequencei

Sequence statusi: Complete.

P45314-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQKLENIKF VITDVDGVLT DGQLHYDANG EAIKSFHVRD GLGIKMLMDA
60 70 80 90 100
DIQVAVLSGR DSPILRRRIA DLGIKLFFLG KLEKETACFD LMKQAGVTAE
110 120 130 140 150
QTAYIGDDSV DLPAFAACGT SFAVADAPIY VKNAVDHVLS THGGKGAFRE
160 170 180
MSDMILQAQG KSSVFDTAQG FLKSVKSMGQ
Length:180
Mass (Da):19,432
Last modified:November 1, 1995 - v1
Checksum:i23CD435E4E83A095
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC23325.1.
PIRiG64174.
RefSeqiNP_439821.1. NC_000907.1.
WP_005665007.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC23325; AAC23325; HI_1679.
GeneIDi950506.
KEGGihin:HI1679.
PATRICi20192109. VBIHaeInf48452_1758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC23325.1.
PIRiG64174.
RefSeqiNP_439821.1. NC_000907.1.
WP_005665007.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J8DX-ray2.30A/B/C/D1-180[»]
1K1EX-ray1.67A/B/C/D/E/F/G/H/I/J/K/L1-180[»]
4HGPX-ray1.80A1-180[»]
ProteinModelPortaliP45314.
SMRiP45314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI1679.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC23325; AAC23325; HI_1679.
GeneIDi950506.
KEGGihin:HI1679.
PATRICi20192109. VBIHaeInf48452_1758.

Phylogenomic databases

eggNOGiENOG4108Z4R. Bacteria.
COG1778. LUCA.
KOiK03270.
OMAiFDENFHE.
PhylomeDBiP45314.

Miscellaneous databases

EvolutionaryTraceiP45314.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR010023. KDO_8-P_phosphatase.
[Graphical view]
PfamiPF08282. Hydrolase_3. 1 hit.
[Graphical view]
PIRSFiPIRSF006118. KDO8-P_Ptase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01670. KdsC-phosphatas. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKDSC_HAEIN
AccessioniPrimary (citable) accession number: P45314
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Cobalt was used in the crystallography experiment but magnesium is likely to be the physiological metal.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  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.