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P45314 (KDSC_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Ordered Locus Names:HI_1679
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

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

Cofactor

Magnesium Probable. Ref.2

Subunit structure

Homotetramer. Ref.3

Miscellaneous

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

Sequence similarities

Belongs to the kdsC family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1801803-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC
PRO_0000201703

Regions

Region14 – 163Substrate binding By similarity
Region37 – 415Substrate binding By similarity
Region58 – 592Substrate binding By similarity

Sites

Metal binding141Magnesium Probable
Metal binding161Magnesium Probable
Metal binding1071Magnesium Probable
Binding site161Substrate By similarity
Binding site601Substrate By similarity
Binding site681Substrate By similarity
Binding site841Substrate By similarity
Binding site1741Substrate; via carbonyl oxygen By similarity

Secondary structure

1 ........................................ 180
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45314 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 23CD435E4E83A095

FASTA18019,432
        10         20         30         40         50         60 
MQQKLENIKF VITDVDGVLT DGQLHYDANG EAIKSFHVRD GLGIKMLMDA DIQVAVLSGR 

        70         80         90        100        110        120 
DSPILRRRIA DLGIKLFFLG KLEKETACFD LMKQAGVTAE QTAYIGDDSV DLPAFAACGT 

       130        140        150        160        170        180 
SFAVADAPIY VKNAVDHVLS THGGKGAFRE MSDMILQAQG KSSVFDTAQG FLKSVKSMGQ

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed: 7542800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]"Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase."
Wu J., Woodard R.W.
J. Biol. Chem. 278:18117-18123(2003) [PubMed: 12639950] [Abstract]
Cited for: FUNCTION AS A KDO 8-P PHOSPHATASE, COFACTOR.
[3]"From structure to function: YrbI from Haemophilus influenzae (HI1679) is a phosphatase."
Parsons J.F., Lim K., Tempczyk A., Krajewski W., Eisenstein E., Herzberg O.
Proteins 46:393-404(2002) [PubMed: 11835514] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH DIVALENT METALS, SUBUNIT, METAL-BINDING.
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC23325.1.
PIRG64174.
RefSeqNP_439821.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP45314.
SMRP45314. Positions 1-180.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID950506.
GenomeReviewsGene locus HI_1679 in contig L42023_GR.
KEGGhin:HI1679.
NMPDRfig|71421.1.peg.1592.
PATRIC20192109. VBIHaeInf48452_1758.
TIGRHI_1679.

Phylogenomic databases

HOGENOMHBG471796.
OMAKTFNTLD.
ProtClustDBCLSK870145.

Enzyme and pathway databases

BioCycHINF71421:HI_1679-MONOMER.

Family and domain databases

InterProIPR023214. HAD-like_dom.
IPR013200. HAD-SF_hydro-like_3.
IPR006549. HAD-SF_hydro_IIIA.
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.
TIGRFAMsTIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01670. YrbI-phosphatas. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKDSC_HAEIN
AccessionPrimary (citable) accession number: P45314
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents