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Reviewed, UniProtKB/Swiss-Prot P45314 (KDOP_HAEIN)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
    EC=3.1.3.45
Alternative name(s):
    KDO 8-P phosphatase
Gene names
Ordered Locus Names: HI1679
OrganismHaemophilus influenzae [Complete proteome] [HAMAP]
Taxonomic identifier727 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the hydrolysis of KDO 8-P to 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.

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
PRO_0000201703

Sites

Metal binding141Magnesium Probable
Metal binding161Magnesium Probable
Metal binding1071Magnesium Probable

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P45314-1 [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, 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), METAL-BINDING.

Cross-references

Sequence databases

L42023 Genomic DNA. Translation: AAC23325.1.
PIRG64174.
RefSeqNP_439821.1.

3D structure databases

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[»]
ModBaseSearch...

Genome annotation databases

GeneID950506.
GenomeReviewsGene locus HI1679 in contig L42023_GR.
KEGGhin:HI1679.
NMPDRfig|71421.1.peg.1592.
TIGRHI1679.

Phylogenomic databases

HOGENOMP45314.
OMAP45314. KTFNTLD.

Enzyme and pathway databases

BioCycHINF71421:HI_1679-MON.
BRENDA3.1.3.45. 109.

Family and domain databases

InterProIPR005834. Dehalogen-like_hydro.
IPR006549. HAD-SF_hydro_IIIA.
IPR010023. Phosphatase_KdsC.
[Graphical view]
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01670. YrbI-phosphatas. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKDOP_HAEIN
AccessionPrimary (citable) accession number: P45314
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents