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A1YYW7

- ALPH_SPHSX

UniProt

A1YYW7 - ALPH_SPHSX

Protein

Alkaline phosphatase PhoK

Gene

phoK

Organism
Sphingomonas sp.
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 30 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    Alkaline phosphatase with broad substrate specificity. Precipitates uranium from alkaline solutions.2 Publications

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.2 Publications

    Cofactori

    Binds 2 zinc ions.1 Publication

    pH dependencei

    Optimum pH is 9.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi49 – 491Zinc 11 Publication
    Active sitei89 – 891Phosphothreonine intermediate1 Publication
    Metal bindingi89 – 891Zinc 11 Publication
    Binding sitei110 – 1101Substrate1 Publication
    Metal bindingi300 – 3001Zinc 21 Publication
    Metal bindingi304 – 3041Zinc 2; via tele nitrogen1 Publication
    Metal bindingi345 – 3451Zinc 11 Publication
    Metal bindingi346 – 3461Zinc 1; via tele nitrogen1 Publication
    Metal bindingi491 – 4911Zinc 2; via tele nitrogen1 Publication

    GO - Molecular functioni

    1. alkaline phosphatase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. dephosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alkaline phosphatase PhoK (EC:3.1.3.1)
    Alternative name(s):
    SPAP protein
    Gene namesi
    Name:phoKImported
    OrganismiSphingomonas sp.
    Taxonomic identifieri28214 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingomonas

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 559540Alkaline phosphatase PhoKPRO_0000392472Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi90 ↔ 1261 Publication
    Disulfide bondi231 ↔ 3141 Publication
    Disulfide bondi545 ↔ 5561 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Expressioni

    Inductioni

    Constitutively expressed.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    559
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi41 – 488
    Helixi53 – 597
    Helixi60 – 623
    Helixi66 – 738
    Beta strandi74 – 818
    Helixi89 – 968
    Helixi102 – 1054
    Beta strandi109 – 1135
    Beta strandi118 – 1203
    Beta strandi123 – 1253
    Helixi152 – 1598
    Beta strandi165 – 1717
    Helixi172 – 1798
    Beta strandi184 – 1896
    Helixi205 – 21814
    Helixi229 – 2346
    Beta strandi238 – 2403
    Beta strandi243 – 2464
    Helixi257 – 2615
    Helixi264 – 28017
    Turni281 – 2844
    Beta strandi285 – 2884
    Beta strandi290 – 2967
    Helixi298 – 3069
    Beta strandi308 – 3103
    Helixi311 – 33323
    Beta strandi338 – 3436
    Helixi352 – 3554
    Turni356 – 3594
    Helixi368 – 3703
    Helixi372 – 38312
    Beta strandi391 – 40212
    Helixi408 – 42417
    Beta strandi428 – 4336
    Helixi434 – 4385
    Helixi447 – 4493
    Helixi452 – 4587
    Turni462 – 4643
    Beta strandi467 – 4726
    Beta strandi476 – 4794
    Helixi496 – 4994
    Beta strandi500 – 5078
    Helixi521 – 5233
    Helixi524 – 5318
    Helixi538 – 5403

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3Q3QX-ray1.95A1-559[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni171 – 1733Substrate binding

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.720.10. 2 hits.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR026263. Alkaline_phosphatase_prok.
    IPR002591. Phosphodiest/P_Trfase.
    [Graphical view]
    PfamiPF01663. Phosphodiest. 1 hit.
    [Graphical view]
    PIRSFiPIRSF031924. Pi-irrepressible_AP. 1 hit.
    SUPFAMiSSF53649. SSF53649. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A1YYW7-1 [UniParc]FASTAAdd to Basket

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    MLKHVAAALL LATAMPVVAQ SPAPAAAPAP AARSIAATPP KLIVAISVDQ    50
    FSADLFSEYR QYYTGGLKRL TSEGAVFPRG YQSHAATETC PGHSTILTGS 100
    RPSRTGIIAN NWFDLDAKRE DKNLYCAEDE SQPGSSSDKY EASPLHLKVP 150
    TLGGRMKAAN PATRVVSVAG KDRAAIMMGG ATADQVWWLG GPQGYVSYKG 200
    VAPTPLVTQV NQAFAQRLAQ PNPGFELPAQ CVSKDFPVQA GNRTVGTGRF 250
    ARDAGDYKGF RISPEQDAMT LAFAAAAIEN MQLGKQAQTD IISIGLSATD 300
    YVGHTFGTEG TESCIQVDRL DTELGAFFDK LDKDGIDYVV VLTADHGGHD 350
    LPERHRMNAM PMEQRVDMAL TPKALNATIA EKAGLPGKKV IWSDGPSGDI 400
    YYDKGLTAAQ RARVETEALK YLRAHPQVQT VFTKAEIAAT PSPSGPPESW 450
    SLIQEARASF YPSRSGDLLL LLKPRVMSIP EQAVMGSVAT HGSPWDTDRR 500
    VPILFWRKGM QHFEQPLGVE TVDILPSLAA LIKLPVPKDQ IDGRCLDLVA 550
    GKDDSCAGQ 559
    Length:559
    Mass (Da):59,982
    Last modified:February 6, 2007 - v1
    Checksum:i0A7A0F7838E1A186
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF143994 Genomic DNA. Translation: ABL96598.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF143994 Genomic DNA. Translation: ABL96598.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3Q3Q X-ray 1.95 A 1-559 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.720.10. 2 hits.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR026263. Alkaline_phosphatase_prok.
    IPR002591. Phosphodiest/P_Trfase.
    [Graphical view ]
    Pfami PF01663. Phosphodiest. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF031924. Pi-irrepressible_AP. 1 hit.
    SUPFAMi SSF53649. SSF53649. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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-11 Publication.
    2. "PhoK alkaline phosphatase."
      Nilgiriwala K.S., Apte S.K.
      Submitted (SEP-2009) to UniProtKB
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: BSAR-11 Publication.
    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.

    Entry informationi

    Entry nameiALPH_SPHSX
    AccessioniPrimary (citable) accession number: A1YYW7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 2010
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 30 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3