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P0AE22 (APHA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Class B acid phosphatase

Short name=CBAP
EC=3.1.3.2
Gene names
Name:aphA
Synonyms:napA, yjbP
Ordered Locus Names:b4055, JW4015
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.8

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.2 Ref.7 Ref.8 Ref.11

Cofactor

Binds 1 magnesium ion per subunit. Ref.9 Ref.10 Ref.11

Enzyme regulation

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-. Ref.2 Ref.8

Subunit structure

Homotetramer. Ref.2 Ref.9 Ref.10 Ref.11

Subcellular location

Periplasm Ref.2.

Sequence similarities

Belongs to the class B bacterial acid phosphatase family.

Biophysicochemical properties

Kinetic parameters:

KM=3.0 µM for 5'-AMP (at 37 degrees Celsius) Ref.2 Ref.8

KM=15.0 µM for 5'-GMP (at 37 degrees Celsius)

KM=15.0 µM for 5'-UMP (at 37 degrees Celsius)

KM=138.0 µM for 5'-CMP (at 37 degrees Celsius)

KM=0.9 µM for 3'-AMP (at 37 degrees Celsius)

KM=1.7 µM for 3'-GMP (at 37 degrees Celsius)

KM=1.2 µM for 3'-UMP (at 37 degrees Celsius)

KM=9.0 µM for 3'-CMP (at 37 degrees Celsius)

KM=0.8 µM for 5'-dAMP (at 37 degrees Celsius)

KM=3.0 µM for 5'-dGMP (at 37 degrees Celsius)

KM=10.0 µM for 5'-dUMP (at 37 degrees Celsius)

KM=35.0 µM for 5'-dCMP (at 37 degrees Celsius)

KM=1.5 µM for 3'-dAMP (at 37 degrees Celsius)

KM=1.6 µM for 3'-dGMP (at 37 degrees Celsius)

KM=0.9 µM for 3'-dUMP (at 37 degrees Celsius)

KM=1.3 µM for 3'-dCMP (at 37 degrees Celsius)

KM=169.0 µM for pNPP (at 37 degrees Celsius)

KM=980.0 µM for ribose 5-phosphate (at 37 degrees Celsius)

KM=1288.0 µM for glucose 6-phosphate (at 37 degrees Celsius)

KM=666.0 µM for beta-glycerol phosphate (at 37 degrees Celsius)

pH dependence:

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

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525Or 23 Ref.6
Chain26 – 237212Class B acid phosphatase
PRO_0000024004

Regions

Region137 – 1382Substrate binding

Sites

Active site691Nucleophile
Active site711Proton donor
Metal binding691Magnesium
Metal binding711Magnesium; via carbonyl oxygen
Metal binding1921Magnesium
Binding site1771Substrate

Secondary structure

........................................... 237
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AE22 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 35C1BFE6DF9E530D

FASTA23726,104
        10         20         30         40         50         60 
MRKITQAISA VCLLFALNSS AVALASSPSP LNPGTNVARL AEQAPIHWVS VAQIENSLAG 

        70         80         90        100        110        120 
RPPMAVGFDI DDTVLFSSPG FWRGKKTFSP ESEDYLKNPV FWEKMNNGWD EFSIPKEVAR 

       130        140        150        160        170        180 
QLIDMHVRRG DAIFFVTGRS PTKTETVSKT LADNFHIPAT NMNPVIFAGD KPGQNTKSQW 

       190        200        210        220        230 
LQDKNIRIFY GDSDNDITAA RDVGARGIRI LRASNSTYKP LPQAGAFGEE VIVNSEY 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS54790.
RefSeqNP_418479.1. NC_000913.3.
YP_492198.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0AE22.
SMRP0AE22. Positions 27-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9116N.
IntActP0AE22. 2 interactions.
MINTMINT-1294190.
STRING511145.b4055.

Proteomic databases

PaxDbP0AE22.
PRIDEP0AE22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77025; AAC77025; b4055.
BAE78057; BAE78057; BAE78057.
GeneID12930343.
948562.
KEGGecj:Y75_p3942.
eco:b4055.
PATRIC32123655. VBIEscCol129921_4176.

Organism-specific databases

EchoBASEEB1878.
EcoGeneEG11934. aphA.

Phylogenomic databases

eggNOGCOG3700.
HOGENOMHOG000270623.
KOK03788.
OMAPEFWEKM.
OrthoDBEOG6HTNVZ.
ProtClustDBPRK11009.

Enzyme and pathway databases

BioCycEcoCyc:APHA-MONOMER.
ECOL316407:JW4015-MONOMER.
MetaCyc:APHA-MONOMER.
BRENDA3.1.3.2. 2026.
SABIO-RKP0AE22.

Gene expression databases

GenevestigatorP0AE22.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR005519. Acid_phosphat_B.
IPR023214. HAD-like_dom.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view]
PfamPF03767. Acid_phosphat_B. 1 hit.
[Graphical view]
PIRSFPIRSF017818. Acid_Ptase_B. 1 hit.
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01672. AphA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0AE22.
PROP0AE22.

Entry information

Entry nameAPHA_ECOLI
AccessionPrimary (citable) accession number: P0AE22
Secondary accession number(s): P32697 expand/collapse secondary AC list , P76787, Q2M6P9, Q57085
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene