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P58683

- APHA_SALTY

UniProt

P58683 - APHA_SALTY

Protein

Class B acid phosphatase

Gene

aphA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (31 Jan 2002)
      Previous versions | rss
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    Functioni

    Dephosphorylates several organic phosphate monoesters such as 3'-UMP, 5'-UMP and pNPP. 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 such as the 2'-, 3-, or 5'-hydroxyls of nucleosides and nucleotides. Also displays significant phosphomutase activity since it is able to catalyze the transfer of the phosphate group of 3'-AMP from the 3'-position both to the 2'- and 5'-positions. One of the physiological functions of the phosphohydrolytic activity of the enzyme is believed to be the scavenging of organic phosphate esters that otherwise cannot pass the cytoplasmic membrane.2 Publications

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Enzyme regulationi

    Nucleosides, and particularly 2'-deoxyribonucleosides, are potent inhibitors of the phosphatase activity. The phosphatase activity is also inhibited by inorganic phosphate and EDTA in vitro.2 Publications

    Kineticsi

    1. KM=0.30 mM for 5'-UMP (at 37 degrees Celsius and pH 6.5)1 Publication

    pH dependencei

    Optimum pH is 5.0-5.5 and 6.5 for the phosphatase activity with 3'-UMP and 5'-UMP as substrate, respectively.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei69 – 691NucleophileBy similarity
    Metal bindingi69 – 691MagnesiumBy similarity
    Active sitei71 – 711Proton donorBy similarity
    Metal bindingi71 – 711Magnesium; via carbonyl oxygenBy similarity
    Binding sitei177 – 1771SubstrateBy similarity
    Metal bindingi192 – 1921MagnesiumBy similarity

    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

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-4280-MONOMER.
    SABIO-RKP58683.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Class B acid phosphatase (EC:3.1.3.2)
    Short name:
    CBAP
    Alternative name(s):
    Non-specific acid phosphatase II
    Gene namesi
    Name:aphA
    Ordered Locus Names:STM4249
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    Subcellular locationi

    Periplasm 1 Publication

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: InterPro

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show a severely decreased growth rate on 5'-UMP as pyrimidine source.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 237214Class B acid phosphatasePRO_0000024009Add
    BLAST

    Proteomic databases

    PaxDbiP58683.
    PRIDEiP58683.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi99287.STM4249.

    Structurei

    3D structure databases

    ProteinModelPortaliP58683.
    SMRiP58683. Positions 27-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP58683.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni137 – 1382Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3700.
    HOGENOMiHOG000270623.
    KOiK03788.
    OMAiPEFWEKM.
    OrthoDBiEOG6HTNVZ.
    PhylomeDBiP58683.

    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.

    P58683-1 [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:January 31, 2002 - v1
    Checksum:i386E11DC84C16269
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL23073.1.
    RefSeqiNP_463114.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL23073; AAL23073; STM4249.
    GeneIDi1255775.
    KEGGistm:STM4249.
    PATRICi32387403. VBISalEnt20916_4469.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL23073.1 .
    RefSeqi NP_463114.1. NC_003197.1.

    3D structure databases

    ProteinModelPortali P58683.
    SMRi P58683. Positions 27-237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM4249.

    Proteomic databases

    PaxDbi P58683.
    PRIDEi P58683.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL23073 ; AAL23073 ; STM4249 .
    GeneIDi 1255775.
    KEGGi stm:STM4249.
    PATRICi 32387403. VBISalEnt20916_4469.

    Phylogenomic databases

    eggNOGi COG3700.
    HOGENOMi HOG000270623.
    KOi K03788.
    OMAi PEFWEKM.
    OrthoDBi EOG6HTNVZ.
    PhylomeDBi P58683.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-4280-MONOMER.
    SABIO-RK P58683.

    Miscellaneous databases

    EvolutionaryTracei P58683.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    2. "Periplasmic phosphatases in Salmonella typhimurium LT2. A biochemical, physiological, and partial genetic analysis of three nucleoside monophosphate dephosphorylating enzymes."
      Uerkvitz W., Beck C.F.
      J. Biol. Chem. 256:382-389(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
      Strain: LT2.
    3. "Periplasmic nonspecific acid phosphatase II from Salmonella typhimurium LT2. Crystallization, detergent reactivation, and phosphotransferase activity."
      Uerkvitz W.
      J. Biol. Chem. 263:15823-15830(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PHOSPHOTRANSFERASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, CRYSTALLIZATION.
      Strain: LT2.

    Entry informationi

    Entry nameiAPHA_SALTY
    AccessioniPrimary (citable) accession number: P58683
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: January 31, 2002
    Last modified: October 1, 2014
    This is version 87 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3