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A1YYW7 (ALPH_SPHSX) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 25. 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

EC=3.1.3.1
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

Precipitates uranium from alkaline solutions. Ref.1

Catalytic activity

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

Subcellular location

Secreted Ref.1.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalkaline phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 559540Alkaline phosphatase
PRO_0000392472

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, SUBCELLULAR LOCATION.
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: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
+Additional computationally mapped references.

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...

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. Alkaline_phosphatase_core. 1 hit.
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: March 6, 2013
This is version 25 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