Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q540U1

- APHA_SALTM

UniProt

Q540U1 - APHA_SALTM

Protein

Class B acid phosphatase

Gene

aphA

Organism
Salmonella typhimurium
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 1 magnesium 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

    1. acid phosphatase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Class B acid phosphataseImported (EC:3.1.3.2Imported1 Publication)
    Short name:
    CBAP
    Gene namesi
    Name:aphAImported
    OrganismiSalmonella typhimurium
    Taxonomic identifieri90371 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

    Subcellular locationi

    Periplasm 1 Publication

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: InterPro

    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

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MKKITLALSA VCLLFTLNHS ANALVSSPST LNPGTNVAKL AEQAPVHWVS    50
    VAQIENSLTG RPPMAVGFDI DDTVLFSSPG FWRGKKTYSP DSDDYLKNPA 100
    FWEKMNNGWD EFSIPKEVAR QLIDMHVRRG DSIYFVTGRS QTKTETVSKT 150
    LADNFHIPAA NMNPVIFAGD KPEQNTKVQW LQEKNMRIFY GDSDNDITAA 200
    RDCGIRGIRI LRAANSTYKP LPQAGAFGEE VIVNSEY 237
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY125468 Genomic DNA. Translation: AAM95781.1.
    AY841758 Genomic DNA. Translation: AAW22868.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY125468 Genomic DNA. Translation: AAM95781.1 .
    AY841758 Genomic DNA. Translation: AAW22868.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z5G X-ray 2.00 A/B/C/D 24-237 [» ]
    1Z5U X-ray 2.30 A/B/C/D 24-237 [» ]
    1Z88 X-ray 2.10 A/B/C/D 24-237 [» ]
    2AUT X-ray 2.25 A/B/C/D 24-237 [» ]
    ProteinModelPortali Q540U1.
    SMRi Q540U1. Positions 27-237.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q540U1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.1000. 1 hit.
    InterProi IPR005519. Acid_phosphat_B.
    IPR023214. HAD-like_dom.
    IPR010025. HAD-SF_ppase_IIIB_AphA.
    [Graphical view ]
    Pfami PF03767. Acid_phosphat_B. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017818. Acid_Ptase_B. 1 hit.
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01672. AphA. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 37 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