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Protein

Class B acid phosphatase

Gene

aphA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mg2+3 PublicationsNote: Binds 1 Mg2+ 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)DescriptionActionsGraphical viewLength
    Active sitei69Nucleophile1
    Metal bindingi69Magnesium1
    Active sitei71Proton donor1
    Metal bindingi71Magnesium; via carbonyl oxygen1
    Binding sitei177Substrate1
    Metal bindingi192Magnesium1

    GO - Molecular functioni

    • acid phosphatase activity Source: EcoCyc
    • cofactor binding Source: EcoCyc
    • metal ion binding Source: UniProtKB-KW
    • phosphoserine phosphatase activity Source: EcoCyc
    Complete GO annotation...

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11934. aphA.

    Subcellular locationi

    • Periplasm 1 Publication

    GO - Cellular componenti

    • outer membrane-bounded periplasmic space Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 25Or 231 PublicationAdd BLAST25
    ChainiPRO_000002400426 – 237Class B acid phosphataseAdd BLAST212

    Proteomic databases

    EPDiP0AE22.
    PaxDbiP0AE22.
    PRIDEiP0AE22.

    Interactioni

    Subunit structurei

    Homotetramer.4 Publications

    Protein-protein interaction databases

    BioGridi4259337. 10 interactors.
    DIPiDIP-9116N.
    IntActiP0AE22. 2 interactors.
    MINTiMINT-1294190.
    STRINGi511145.b4055.

    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 – 106Combined sources8
    Helixi109 – 112Combined sources4
    Beta strandi113 – 115Combined sources3
    Helixi117 – 129Combined sources13
    Beta strandi132 – 137Combined sources6
    Helixi147 – 154Combined sources8
    Turni159 – 161Combined sources3
    Beta strandi169 – 171Combined sources3
    Helixi178 – 183Combined sources6
    Beta strandi186 – 193Combined sources8
    Helixi194 – 202Combined sources9
    Beta strandi206 – 209Combined sources4
    Turni224 – 227Combined sources4
    Beta strandi230 – 232Combined sources3
    Turni233 – 236Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    SMRiP0AE22.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AE22.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni137 – 138Substrate binding2

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105F0S. Bacteria.
    COG3700. LUCA.
    HOGENOMiHOG000270623.
    KOiK03788.
    OMAiPEFWEKM.

    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.

    P0AE22-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRKITQAISA VCLLFALNSS AVALASSPSP LNPGTNVARL AEQAPIHWVS
    60 70 80 90 100
    VAQIENSLAG RPPMAVGFDI DDTVLFSSPG FWRGKKTFSP ESEDYLKNPV
    110 120 130 140 150
    FWEKMNNGWD EFSIPKEVAR QLIDMHVRRG DAIFFVTGRS PTKTETVSKT
    160 170 180 190 200
    LADNFHIPAT NMNPVIFAGD KPGQNTKSQW LQDKNIRIFY GDSDNDITAA
    210 220 230
    RDVGARGIRI LRASNSTYKP LPQAGAFGEE VIVNSEY
    Length:237
    Mass (Da):26,104
    Last modified:December 6, 2005 - v1
    Checksum:i35C1BFE6DF9E530D
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.
    WP_001226928.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77025; AAC77025; b4055.
    BAE78057; BAE78057; BAE78057.
    GeneIDi948562.
    KEGGiecj:JW4015.
    eco:b4055.
    PATRICi32123655. VBIEscCol129921_4176.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.
    WP_001226928.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    SMRiP0AE22.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259337. 10 interactors.
    DIPiDIP-9116N.
    IntActiP0AE22. 2 interactors.
    MINTiMINT-1294190.
    STRINGi511145.b4055.

    Proteomic databases

    EPDiP0AE22.
    PaxDbiP0AE22.
    PRIDEiP0AE22.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC77025; AAC77025; b4055.
    BAE78057; BAE78057; BAE78057.
    GeneIDi948562.
    KEGGiecj:JW4015.
    eco:b4055.
    PATRICi32123655. VBIEscCol129921_4176.

    Organism-specific databases

    EchoBASEiEB1878.
    EcoGeneiEG11934. aphA.

    Phylogenomic databases

    eggNOGiENOG4105F0S. Bacteria.
    COG3700. LUCA.
    HOGENOMiHOG000270623.
    KOiK03788.
    OMAiPEFWEKM.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP0AE22.
    PROiP0AE22.

    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_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: November 2, 2016
    This is version 102 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

    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.