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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 (PubMed:14501135, PubMed:17570338). 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 (By similarity).By similarity2 Publications

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)DescriptionActionsGraphical viewLength
    Active sitei69Nucleophile1 Publication1
    Metal bindingi69Magnesium1 Publication1
    Active sitei71Proton donor1 Publication1
    Metal bindingi71Magnesium; via carbonyl oxygen1 Publication1
    Binding sitei177Substrate1 Publication1
    Metal bindingi192Magnesium1 Publication1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    SABIO-RKQ540U1.

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella

    Subcellular locationi

    • Periplasm 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi177K → N: 40-fold reduction in phosphatase activity. 5.6-fold increase in KM for pNPP in presence of 1 mM MgCl(2). 1 Publication1
    Mutagenesisi177K → R: 20-fold reduction in phosphatase activity. Nearly 2-fold increase in KM for pNPP in presence of 1 mM MgCl(2). 1 Publication1
    Mutagenesisi196D → 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 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 231 PublicationAdd BLAST23
    ChainiPRO_000041492224 – 237Class B acid phosphatase1 PublicationAdd BLAST214

    Proteomic databases

    PaxDbiQ540U1.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    STRINGi99287.STM4249.

    Structurei

    Secondary structure

    1237
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi37 – 41Combined sources5
    Beta strandi47 – 49Combined sources3
    Helixi51 – 57Combined sources7
    Turni58 – 60Combined sources3
    Beta strandi65 – 68Combined sources4
    Turni72 – 74Combined sources3
    Helixi78 – 88Combined sources11
    Helixi94 – 97Combined sources4
    Helixi99 – 105Combined sources7
    Turni106 – 108Combined sources3
    Helixi109 – 112Combined sources4
    Helixi117 – 129Combined sources13
    Beta strandi132 – 137Combined sources6
    Helixi147 – 154Combined sources8
    Turni159 – 161Combined sources3
    Helixi177 – 183Combined sources7
    Beta strandi186 – 193Combined sources8
    Helixi194 – 203Combined sources10
    Beta strandi205 – 209Combined sources5
    Turni225 – 227Combined sources3
    Beta strandi230 – 232Combined sources3
    Turni233 – 236Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni137 – 138Substrate binding1 Publication2

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105F0S. Bacteria.
    COG3700. LUCA.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR005519. Acid_phosphat_B-like.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti118V → A in AAW22868 (PubMed:14501135).Curated1

    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_MATL01000020.1.

    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_MATL01000020.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi99287.STM4249.

    Proteomic databases

    PaxDbiQ540U1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG4105F0S. Bacteria.
    COG3700. LUCA.

    Enzyme and pathway databases

    SABIO-RKQ540U1.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR005519. Acid_phosphat_B-like.
    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...

    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: November 2, 2016
    This is version 50 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

    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 one 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.