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Protein

Class B acid phosphatase

Gene

aphA

Organism
Salmonella typhimurium
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dephosphorylates several organic phosphate monoesters. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds (Probable).1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

  1. KM=0.15 mM for pNPP (in the presence of 1 mM MgCl2 at 37 degrees Celsius and pH 5.6)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei69 – 691Nucleophile1 Publication
    Metal bindingi69 – 691Magnesium1 Publication
    Active sitei71 – 711Proton donor1 Publication
    Metal bindingi71 – 711Magnesium; via carbonyl oxygen1 Publication
    Binding sitei177 – 1771Substrate1 Publication
    Metal bindingi192 – 1921Magnesium1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Class B acid phosphataseImported (EC:3.1.3.21 PublicationImported)
    Short name:
    CBAP
    Gene namesi
    Name:aphAImported
    OrganismiSalmonella typhimurium
    Taxonomic identifieri90371 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

    Subcellular locationi

    • Periplasm 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi177 – 1771K → N: 40-fold reduction in phosphatase activity. 5.6-fold increase in KM for pNPP in presence of 1 mM MgCl(2). 1 Publication
    Mutagenesisi177 – 1771K → R: 20-fold reduction in phosphatase activity. Nearly 2-fold increase in KM for pNPP in presence of 1 mM MgCl(2). 1 Publication
    Mutagenesisi196 – 1961D → N: 6-fold reduction in phosphatase activity. 10000-fold decrease in affinity for Mg(2+). 18-fold increase in KM for pNPP in presence of 1 mM MgCl(2). KM is 0.79 mM for pNPP in the presence of 10 mM MgCl(2). 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23231 PublicationAdd
    BLAST
    Chaini24 – 237214Class B acid phosphatase1 PublicationPRO_0000414922Add
    BLAST

    Proteomic databases

    PRIDEiQ540U1.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    STRINGi99287.STM4249.

    Structurei

    Secondary structure

    1
    237
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi37 – 415Combined sources
    Beta strandi47 – 493Combined sources
    Helixi51 – 577Combined sources
    Turni58 – 603Combined sources
    Beta strandi65 – 684Combined sources
    Turni72 – 743Combined sources
    Helixi78 – 8811Combined sources
    Helixi94 – 974Combined sources
    Helixi99 – 1057Combined sources
    Turni106 – 1083Combined sources
    Helixi109 – 1124Combined sources
    Helixi117 – 12913Combined sources
    Beta strandi132 – 1376Combined sources
    Helixi147 – 1548Combined sources
    Turni159 – 1613Combined sources
    Helixi177 – 1837Combined sources
    Beta strandi186 – 1938Combined sources
    Helixi194 – 20310Combined sources
    Beta strandi205 – 2095Combined sources
    Turni225 – 2273Combined sources
    Beta strandi230 – 2323Combined sources
    Turni233 – 2364Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z5GX-ray2.00A/B/C/D24-237[»]
    1Z5UX-ray2.30A/B/C/D24-237[»]
    1Z88X-ray2.10A/B/C/D24-237[»]
    2AUTX-ray2.25A/B/C/D24-237[»]
    ProteinModelPortaliQ540U1.
    SMRiQ540U1. Positions 27-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni137 – 1382Substrate binding1 Publication

    Sequence similaritiesi

    Belongs to the class B bacterial acid phosphatase family.By similarity

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR005519. Acid_phosphat_B.
    IPR023214. HAD-like_dom.
    IPR010025. HAD-SF_ppase_IIIB_AphA.
    [Graphical view]
    PfamiPF03767. Acid_phosphat_B. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017818. Acid_Ptase_B. 1 hit.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01672. AphA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q540U1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKITLALSA VCLLFTLNHS ANALVSSPST LNPGTNVAKL AEQAPVHWVS
    60 70 80 90 100
    VAQIENSLTG RPPMAVGFDI DDTVLFSSPG FWRGKKTYSP DSDDYLKNPA
    110 120 130 140 150
    FWEKMNNGWD EFSIPKEVAR QLIDMHVRRG DSIYFVTGRS QTKTETVSKT
    160 170 180 190 200
    LADNFHIPAA NMNPVIFAGD KPEQNTKVQW LQEKNMRIFY GDSDNDITAA
    210 220 230
    RDCGIRGIRI LRAANSTYKP LPQAGAFGEE VIVNSEY
    Length:237
    Mass (Da):26,315
    Last modified:May 24, 2005 - v1
    Checksum:i386E11DC84C16269
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti118 – 1181V → A in AAW22868 (PubMed:14501135).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY125468 Genomic DNA. Translation: AAM95781.1.
    AY841758 Genomic DNA. Translation: AAW22868.1.
    RefSeqiWP_000724435.1. NZ_JRGW01000010.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY125468 Genomic DNA. Translation: AAM95781.1.
    AY841758 Genomic DNA. Translation: AAW22868.1.
    RefSeqiWP_000724435.1. NZ_JRGW01000010.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z5GX-ray2.00A/B/C/D24-237[»]
    1Z5UX-ray2.30A/B/C/D24-237[»]
    1Z88X-ray2.10A/B/C/D24-237[»]
    2AUTX-ray2.25A/B/C/D24-237[»]
    ProteinModelPortaliQ540U1.
    SMRiQ540U1. Positions 27-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi99287.STM4249.

    Proteomic databases

    PRIDEiQ540U1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR005519. Acid_phosphat_B.
    IPR023214. HAD-like_dom.
    IPR010025. HAD-SF_ppase_IIIB_AphA.
    [Graphical view]
    PfamiPF03767. Acid_phosphat_B. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017818. Acid_Ptase_B. 1 hit.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01672. AphA. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Expression, purification, crystallization and preliminary X-ray diffraction studies of recombinant class B non-specific acid phosphatase of Salmonella typhimurium."
      Makde R.D., Kumar V., Gupta G.D., Jasti J., Singh T.P., Mahajan S.K.
      Acta Crystallogr. D 59:1849-1852(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-38 AND 40-46, FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, CRYSTALLIZATION.
      Strain: MD6001Imported.
    2. "Structural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein."
      Makde R.D., Gupta G.D., Mahajan S.K., Kumar V.
      Arch. Biochem. Biophys. 464:70-79(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-237 OF WILD-TYPE AND MUTANTS ARG/ASN-177 IN COMPLEXES WITH CAMP; PHOSPHATE AND MAGNESIUM IONS, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF LYS-177 AND ASP-196.
      Strain: MD6001.

    Entry informationi

    Entry nameiAPHA_SALTM
    AccessioniPrimary (citable) accession number: Q540U1
    Secondary accession number(s): Q5MB24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: May 24, 2005
    Last modified: June 24, 2015
    This is version 40 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, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.