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A1YYW7 (ALPH_SPHSX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alkaline phosphatase PhoK

EC=3.1.3.1
Alternative name(s):
SPAP protein
Gene names
Name:phoK
OrganismSphingomonas sp.
Taxonomic identifier28214 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingomonas

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alkaline phosphatase with broad substrate specificity. Precipitates uranium from alkaline solutions. Ref.1 Ref.4

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.1 Ref.4

Cofactor

Binds 2 zinc ions. Ref.4

Subunit structure

Monomer. Ref.4

Subcellular location

Secreted Ref.1.

Induction

Constitutively expressed. Ref.1

Biophysicochemical properties

pH dependence:

Optimum pH is 9.0. Ref.1

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Phosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processdephosphorylation

Inferred from direct assay Ref.1Ref.4. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionalkaline phosphatase activity

Inferred from direct assay Ref.1Ref.4. Source: UniProtKB

metal ion binding

Inferred from direct assay Ref.4. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 559540Alkaline phosphatase PhoK
PRO_0000392472

Regions

Region171 – 1733Substrate binding

Sites

Active site891Phosphothreonine intermediate Probable
Metal binding491Zinc 1
Metal binding891Zinc 1
Metal binding3001Zinc 2
Metal binding3041Zinc 2; via tele nitrogen
Metal binding3451Zinc 1
Metal binding3461Zinc 1; via tele nitrogen
Metal binding4911Zinc 2; via tele nitrogen
Binding site1101Substrate

Amino acid modifications

Disulfide bond90 ↔ 126 Ref.4
Disulfide bond231 ↔ 314 Ref.4
Disulfide bond545 ↔ 556 Ref.4

Secondary structure

................................................................................. 559
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A1YYW7 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 0A7A0F7838E1A186

FASTA55959,982
        10         20         30         40         50         60 
MLKHVAAALL LATAMPVVAQ SPAPAAAPAP AARSIAATPP KLIVAISVDQ FSADLFSEYR 

        70         80         90        100        110        120 
QYYTGGLKRL TSEGAVFPRG YQSHAATETC PGHSTILTGS RPSRTGIIAN NWFDLDAKRE 

       130        140        150        160        170        180 
DKNLYCAEDE SQPGSSSDKY EASPLHLKVP TLGGRMKAAN PATRVVSVAG KDRAAIMMGG 

       190        200        210        220        230        240 
ATADQVWWLG GPQGYVSYKG VAPTPLVTQV NQAFAQRLAQ PNPGFELPAQ CVSKDFPVQA 

       250        260        270        280        290        300 
GNRTVGTGRF ARDAGDYKGF RISPEQDAMT LAFAAAAIEN MQLGKQAQTD IISIGLSATD 

       310        320        330        340        350        360 
YVGHTFGTEG TESCIQVDRL DTELGAFFDK LDKDGIDYVV VLTADHGGHD LPERHRMNAM 

       370        380        390        400        410        420 
PMEQRVDMAL TPKALNATIA EKAGLPGKKV IWSDGPSGDI YYDKGLTAAQ RARVETEALK 

       430        440        450        460        470        480 
YLRAHPQVQT VFTKAEIAAT PSPSGPPESW SLIQEARASF YPSRSGDLLL LLKPRVMSIP 

       490        500        510        520        530        540 
EQAVMGSVAT HGSPWDTDRR VPILFWRKGM QHFEQPLGVE TVDILPSLAA LIKLPVPKDQ 

       550 
IDGRCLDLVA GKDDSCAGQ 

« Hide

References

[1]"Cloning and overexpression of alkaline phosphatase PhoK from Sphingomonas sp. strain BSAR-1 for bioprecipitation of uranium from alkaline solutions."
Nilgiriwala K.S., Alahari A., Rao A.S., Apte S.K.
Appl. Environ. Microbiol. 74:5516-5523(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION.
Strain: BSAR-1.
[2]"PhoK alkaline phosphatase."
Nilgiriwala K.S., Apte S.K.
Submitted (SEP-2009) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Strain: BSAR-1.
[3]"Crystallization and preliminary X-ray crystallographic analysis of PhoK, an extracellular alkaline phosphatase from Sphingomonas sp. BSAR-1."
Nilgiriwala K.S., Bihani S.C., Das A., Prashar V., Kumar M., Ferrer J.L., Apte S.K., Hosur M.V.
Acta Crystallogr. F 65:917-919(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
Strain: BSAR-1.
[4]"X-ray structure reveals a new class and provides insight into evolution of alkaline phosphatases."
Bihani S.C., Das A., Nilgiriwala K.S., Prashar V., Pirocchi M., Apte S.K., Ferrer J.L., Hosur M.V.
PLoS ONE 6:E22767-E22767(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC AND SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, DISULFIDE BONDS.
Strain: BSAR-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF143994 Genomic DNA. Translation: ABL96598.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q3QX-ray1.95A1-559[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.720.10. 2 hits.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR026263. Alkaline_phosphatase_prok.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PfamPF01663. Phosphodiest. 1 hit.
[Graphical view]
PIRSFPIRSF031924. Pi-irrepressible_AP. 1 hit.
SUPFAMSSF53649. SSF53649. 2 hits.
ProtoNetSearch...

Entry information

Entry nameALPH_SPHSX
AccessionPrimary (citable) accession number: A1YYW7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references