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P0AE22

- APHA_ECOLI

UniProt

P0AE22 - APHA_ECOLI

Protein

Class B acid phosphatase

Gene

aphA

Organism
Escherichia coli (strain K12)
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 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Dephosphorylates several organic phosphate monoesters including 3'- and 5'-nucleotides, 2'-deoxy-5'-nucleotides, pNPP, phenyl phosphate, glycerol 2-phosphate, ribose 5-phosphate, O-phospho-L-amino acids and phytic acid, showing the highest activity with aryl phosphoesters (pNPP, phenyl phosphate and O-phospho-L-tyrosine), and to a lesser extent with 3'- and 5'-nucleotides. No activity toward ATP, phosphodiesters, glycerol-1-phosphate, glucose 1-phosphate, glucose 6-phosphate, NADP, GTP or 3',5'-cAMP, ADP or ATP. 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. Capable of transferring phosphate from either pNPP or UMP to adenosine or uridine. Does not exhibit nucleotide phosphomutase activity.2 Publications

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.4 Publications

    Cofactori

    Binds 1 magnesium ion per subunit.3 Publications

    Enzyme regulationi

    Activated by ethanol. Inhibited strongly by EDTA and more weakly by other divalent ions chelators 1,10-phenanthroline, EGTA and dipicolinic acid. Inhibited also by nucleosides, inorganic phosphate and Ca2+. Unaffected by F-.2 Publications

    Kineticsi

    1. KM=3.0 µM for 5'-AMP (at 37 degrees Celsius)2 Publications
    2. KM=15.0 µM for 5'-GMP (at 37 degrees Celsius)2 Publications
    3. KM=15.0 µM for 5'-UMP (at 37 degrees Celsius)2 Publications
    4. KM=138.0 µM for 5'-CMP (at 37 degrees Celsius)2 Publications
    5. KM=0.9 µM for 3'-AMP (at 37 degrees Celsius)2 Publications
    6. KM=1.7 µM for 3'-GMP (at 37 degrees Celsius)2 Publications
    7. KM=1.2 µM for 3'-UMP (at 37 degrees Celsius)2 Publications
    8. KM=9.0 µM for 3'-CMP (at 37 degrees Celsius)2 Publications
    9. KM=0.8 µM for 5'-dAMP (at 37 degrees Celsius)2 Publications
    10. KM=3.0 µM for 5'-dGMP (at 37 degrees Celsius)2 Publications
    11. KM=10.0 µM for 5'-dUMP (at 37 degrees Celsius)2 Publications
    12. KM=35.0 µM for 5'-dCMP (at 37 degrees Celsius)2 Publications
    13. KM=1.5 µM for 3'-dAMP (at 37 degrees Celsius)2 Publications
    14. KM=1.6 µM for 3'-dGMP (at 37 degrees Celsius)2 Publications
    15. KM=0.9 µM for 3'-dUMP (at 37 degrees Celsius)2 Publications
    16. KM=1.3 µM for 3'-dCMP (at 37 degrees Celsius)2 Publications
    17. KM=169.0 µM for pNPP (at 37 degrees Celsius)2 Publications
    18. KM=980.0 µM for ribose 5-phosphate (at 37 degrees Celsius)2 Publications
    19. KM=1288.0 µM for glucose 6-phosphate (at 37 degrees Celsius)2 Publications
    20. KM=666.0 µM for beta-glycerol phosphate (at 37 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 6-6.5 with 5'-AMP as substrate, and pH 5.5-6 with 3'-AMP or pNPP as substrate.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei69 – 691Nucleophile
    Metal bindingi69 – 691Magnesium
    Active sitei71 – 711Proton donor
    Metal bindingi71 – 711Magnesium; via carbonyl oxygen
    Binding sitei177 – 1771Substrate
    Metal bindingi192 – 1921Magnesium

    GO - Molecular functioni

    1. acid phosphatase activity Source: EcoCyc
    2. cofactor binding Source: EcoCyc
    3. metal ion binding Source: UniProtKB-KW
    4. phosphoserine phosphatase activity Source: EcoCyc

    GO - Biological processi

    1. dephosphorylation Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:APHA-MONOMER.
    ECOL316407:JW4015-MONOMER.
    MetaCyc:APHA-MONOMER.
    BRENDAi3.1.3.2. 2026.
    SABIO-RKP0AE22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Class B acid phosphatase (EC:3.1.3.2)
    Short name:
    CBAP
    Gene namesi
    Name:aphA
    Synonyms:napA, yjbP
    Ordered Locus Names:b4055, JW4015
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11934. aphA.

    Subcellular locationi

    Periplasm 1 Publication

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: EcoCyc

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Or 231 PublicationAdd
    BLAST
    Chaini26 – 237212Class B acid phosphatasePRO_0000024004Add
    BLAST

    Proteomic databases

    PaxDbiP0AE22.
    PRIDEiP0AE22.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AE22.

    Interactioni

    Subunit structurei

    Homotetramer.4 Publications

    Protein-protein interaction databases

    DIPiDIP-9116N.
    IntActiP0AE22. 2 interactions.
    MINTiMINT-1294190.
    STRINGi511145.b4055.

    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 – 1068
    Helixi109 – 1124
    Beta strandi113 – 1153
    Helixi117 – 12913
    Beta strandi132 – 1376
    Helixi147 – 1548
    Turni159 – 1613
    Beta strandi169 – 1713
    Helixi178 – 1836
    Beta strandi186 – 1938
    Helixi194 – 2029
    Beta strandi206 – 2094
    Turni224 – 2274
    Beta strandi230 – 2323
    Turni233 – 2364

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N8NX-ray1.69A26-237[»]
    1N9KX-ray2.20A/B26-237[»]
    1RMQX-ray2.00A/B26-237[»]
    1RMTX-ray1.40A/B/C/D26-237[»]
    1RMYX-ray1.75A/B26-237[»]
    2B82X-ray1.25A/B27-237[»]
    2B8JX-ray2.03A/B27-237[»]
    2G1AX-ray2.00A/B26-237[»]
    2HEGX-ray1.50A/B27-237[»]
    2HF7X-ray1.60A/B27-237[»]
    3CZ4X-ray1.70A26-237[»]
    ProteinModelPortaliP0AE22.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AE22.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3700.
    HOGENOMiHOG000270623.
    KOiK03788.
    OMAiPEFWEKM.
    OrthoDBiEOG6HTNVZ.

    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.

    P0AE22-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKITQAISA VCLLFALNSS AVALASSPSP LNPGTNVARL AEQAPIHWVS    50
    VAQIENSLAG RPPMAVGFDI DDTVLFSSPG FWRGKKTFSP ESEDYLKNPV 100
    FWEKMNNGWD EFSIPKEVAR QLIDMHVRRG DAIFFVTGRS PTKTETVSKT 150
    LADNFHIPAT NMNPVIFAGD KPGQNTKSQW LQDKNIRIFY GDSDNDITAA 200
    RDVGARGIRI LRASNSTYKP LPQAGAFGEE VIVNSEY 237
    Length:237
    Mass (Da):26,104
    Last modified:December 6, 2005 - v1
    Checksum:i35C1BFE6DF9E530D
    GO

    Sequence cautioni

    The sequence AAC43149.1 differs from that shown. Reason: Frameshift at position 62.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51210 Genomic DNA. Translation: AAA96322.1.
    X86971 Genomic DNA. Translation: CAA60534.1.
    U00006 Genomic DNA. Translation: AAC43149.1. Frameshift.
    U00096 Genomic DNA. Translation: AAC77025.1.
    AP009048 Genomic DNA. Translation: BAE78057.1.
    PIRiS54790.
    RefSeqiNP_418479.1. NC_000913.3.
    YP_492198.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77025; AAC77025; b4055.
    BAE78057; BAE78057; BAE78057.
    GeneIDi12930343.
    948562.
    KEGGiecj:Y75_p3942.
    eco:b4055.
    PATRICi32123655. VBIEscCol129921_4176.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51210 Genomic DNA. Translation: AAA96322.1 .
    X86971 Genomic DNA. Translation: CAA60534.1 .
    U00006 Genomic DNA. Translation: AAC43149.1 . Frameshift.
    U00096 Genomic DNA. Translation: AAC77025.1 .
    AP009048 Genomic DNA. Translation: BAE78057.1 .
    PIRi S54790.
    RefSeqi NP_418479.1. NC_000913.3.
    YP_492198.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N8N X-ray 1.69 A 26-237 [» ]
    1N9K X-ray 2.20 A/B 26-237 [» ]
    1RMQ X-ray 2.00 A/B 26-237 [» ]
    1RMT X-ray 1.40 A/B/C/D 26-237 [» ]
    1RMY X-ray 1.75 A/B 26-237 [» ]
    2B82 X-ray 1.25 A/B 27-237 [» ]
    2B8J X-ray 2.03 A/B 27-237 [» ]
    2G1A X-ray 2.00 A/B 26-237 [» ]
    2HEG X-ray 1.50 A/B 27-237 [» ]
    2HF7 X-ray 1.60 A/B 27-237 [» ]
    3CZ4 X-ray 1.70 A 26-237 [» ]
    ProteinModelPortali P0AE22.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9116N.
    IntActi P0AE22. 2 interactions.
    MINTi MINT-1294190.
    STRINGi 511145.b4055.

    Proteomic databases

    PaxDbi P0AE22.
    PRIDEi P0AE22.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77025 ; AAC77025 ; b4055 .
    BAE78057 ; BAE78057 ; BAE78057 .
    GeneIDi 12930343.
    948562.
    KEGGi ecj:Y75_p3942.
    eco:b4055.
    PATRICi 32123655. VBIEscCol129921_4176.

    Organism-specific databases

    EchoBASEi EB1878.
    EcoGenei EG11934. aphA.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci EcoCyc:APHA-MONOMER.
    ECOL316407:JW4015-MONOMER.
    MetaCyc:APHA-MONOMER.
    BRENDAi 3.1.3.2. 2026.
    SABIO-RK P0AE22.

    Miscellaneous databases

    EvolutionaryTracei P0AE22.
    PROi P0AE22.

    Gene expression databases

    Genevestigatori P0AE22.

    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. Marquez S.M., Gumport R.I.
      Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. "Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product."
      Thaller M.C., Schippa S., Bonci A., Cresti S., Rossolini G.M.
      FEMS Microbiol. Lett. 146:191-198(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT.
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-37.
      Strain: K12 / EMG2.
    7. "Expression, purification, crystallization and preliminary X-ray characterization of the class B acid phosphatase (AphA) from Escherichia coli."
      Forleo C., Benvenuti M., Calderone V., Schippa S., Docquier J.D., Thaller M.C., Rossolini G.M., Mangani S.
      Acta Crystallogr. D 59:1058-1060(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / MG1655 / ATCC 47076.
    8. "Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655."
      Passariello C., Forleo C., Micheli V., Schippa S., Leone R., Mangani S., Thaller M.C., Rossolini G.M.
      Biochim. Biophys. Acta 1764:13-19(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
      Strain: K12 / MG1655 / ATCC 47076.
    9. "The first structure of a bacterial class B acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold."
      Calderone V., Forleo C., Benvenuti M., Cristina Thaller M., Maria Rossolini G., Mangani S.
      J. Mol. Biol. 335:761-773(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 26-237 IN COMPLEXES WITH MAGNESIUM IONS, COFACTOR, SUBUNIT.
      Strain: K12 / MG1655 / ATCC 47076.
    10. "A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases."
      Calderone V., Forleo C., Benvenuti M., Thaller M.C., Rossolini G.M., Mangani S.
      J. Mol. Biol. 355:708-721(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 26-237 IN COMPLEXES WITH REACTION INTERMEDIATE ANALOG; REACTION PRODUCTS; PHOSPHATE AND MAGNESIUM IONS, COFACTOR, REACTION MECHANISM, SUBUNIT.
      Strain: K12 / MG1655 / ATCC 47076.
    11. "Structural insights into the catalytic mechanism of the bacterial class B phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases."
      Leone R., Cappelletti E., Benvenuti M., Lentini G., Thaller M.C., Mangani S.
      J. Mol. Biol. 384:478-488(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 26-237 IN COMPLEXES WITH SUBSTRATE ANALOG INHIBITOR; TRANSITION STATE ANALOG; REACTION INTERMEDIATE ANALOG AND MAGNESIUM IONS, CATALYTIC ACTIVITY, COFACTOR, REACTION MECHANISM, SUBUNIT.
      Strain: K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiAPHA_ECOLI
    AccessioniPrimary (citable) accession number: P0AE22
    Secondary accession number(s): P32697
    , P76787, Q2M6P9, Q57085
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3