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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141MagnesiumCurated
Metal bindingi16 – 161MagnesiumCurated
Binding sitei16 – 161SubstrateBy similarity
Binding sitei60 – 601SubstrateBy similarity
Binding sitei68 – 681SubstrateBy similarity
Binding sitei84 – 841SubstrateBy similarity
Metal bindingi107 – 1071MagnesiumCurated
Binding sitei174 – 1741Substrate; via carbonyl oxygenBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1801803-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsCPRO_0000201703Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi71421.HI1679.

Structurei

Secondary structure

1
180
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Beta strandi10 – 145Combined sources
Turni16 – 183Combined sources
Beta strandi22 – 276Combined sources
Beta strandi30 – 378Combined sources
Helixi38 – 4912Combined sources
Beta strandi53 – 597Combined sources
Helixi63 – 7210Combined sources
Beta strandi76 – 805Combined sources
Helixi84 – 9512Combined sources
Helixi99 – 1013Combined sources
Beta strandi102 – 1065Combined sources
Helixi109 – 1113Combined sources
Helixi112 – 1176Combined sources
Beta strandi118 – 1236Combined sources
Helixi129 – 1324Combined sources
Beta strandi135 – 1384Combined sources
Turni143 – 1464Combined sources
Helixi147 – 15812Combined sources
Helixi163 – 1664Combined sources
Helixi168 – 1747Combined sources
Helixi175 – 1773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45314.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 163Substrate bindingBy similarity
Regioni37 – 415Substrate bindingBy similarity
Regioni58 – 592Substrate bindingBy similarity

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
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. Positions 1-180.
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: September 7, 2016
This is version 118 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.