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P0AE22

- APHA_ECOLI

UniProt

P0AE22 - APHA_ECOLI

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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

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 Mg(2+) 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
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 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
Complete GO annotation...

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 – 415Combined sources
Beta strandi47 – 493Combined sources
Helixi51 – 577Combined sources
Turni58 – 603Combined sources
Beta strandi65 – 684Combined sources
Turni72 – 743Combined sources
Helixi78 – 8811Combined sources
Helixi94 – 974Combined sources
Helixi99 – 1068Combined sources
Helixi109 – 1124Combined sources
Beta strandi113 – 1153Combined sources
Helixi117 – 12913Combined sources
Beta strandi132 – 1376Combined sources
Helixi147 – 1548Combined sources
Turni159 – 1613Combined sources
Beta strandi169 – 1713Combined sources
Helixi178 – 1836Combined sources
Beta strandi186 – 1938Combined sources
Helixi194 – 2029Combined sources
Beta strandi206 – 2094Combined sources
Turni224 – 2274Combined sources
Beta strandi230 – 2323Combined sources
Turni233 – 2364Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
SMRiP0AE22. Positions 27-237.
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

        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 AAC43149.1 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.
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:
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 .
PIRi S54790.
RefSeqi NP_418479.1. NC_000913.3.
YP_492198.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
SMRi P0AE22. Positions 27-237.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 89 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