Class B acid phosphatase precursor - Escherichia coli (strain K12)

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P0AE22 (APHA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	237 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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: K_M=3.0 µM for 5'-AMP (at 37 degrees Celsius) Ref.2 Ref.8 K_M=15.0 µM for 5'-GMP (at 37 degrees Celsius) K_M=15.0 µM for 5'-UMP (at 37 degrees Celsius) K_M=138.0 µM for 5'-CMP (at 37 degrees Celsius) K_M=0.9 µM for 3'-AMP (at 37 degrees Celsius) K_M=1.7 µM for 3'-GMP (at 37 degrees Celsius) K_M=1.2 µM for 3'-UMP (at 37 degrees Celsius) K_M=9.0 µM for 3'-CMP (at 37 degrees Celsius) K_M=0.8 µM for 5'-dAMP (at 37 degrees Celsius) K_M=3.0 µM for 5'-dGMP (at 37 degrees Celsius) K_M=10.0 µM for 5'-dUMP (at 37 degrees Celsius) K_M=35.0 µM for 5'-dCMP (at 37 degrees Celsius) K_M=1.5 µM for 3'-dAMP (at 37 degrees Celsius) K_M=1.6 µM for 3'-dGMP (at 37 degrees Celsius) K_M=0.9 µM for 3'-dUMP (at 37 degrees Celsius) K_M=1.3 µM for 3'-dCMP (at 37 degrees Celsius) K_M=169.0 µM for pNPP (at 37 degrees Celsius) K_M=980.0 µM for ribose 5-phosphate (at 37 degrees Celsius) K_M=1288.0 µM for glucose 6-phosphate (at 37 degrees Celsius) K_M=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.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro
Molecular_function	acid phosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

Or 23 Ref.6

Chain

26 – 237

212

Class B acid phosphatase

PRO_0000024004

Regions

Region

137 – 138

Substrate binding

Sites

Active site

Nucleophile

Active site

Proton donor

Metal binding

Magnesium

Metal binding

Magnesium; via carbonyl oxygen

Metal binding

192

Magnesium

Binding site

177

Substrate

Secondary structure

237

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AE22 [UniParc].

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

FASTA

237

26,104

        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' referencesShow '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 277:1453-1474(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, 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.

PIR

S54790.

RefSeq

NP_418479.1. NC_000913.2.
YP_492198.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0AE22.

SMR

P0AE22. Positions 27-237.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AE22. 2 interactions.

MINT

MINT-1294190.

STRING

511145.b4055.

Proteomic databases

PaxDb

P0AE22.

PRIDE

P0AE22.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77025; AAC77025; b4055.
BAE78057; BAE78057; BAE78057.

GeneID

12930343.
948562.

KEGG

ecj:Y75_p3942.
eco:b4055.

PATRIC

32123655. VBIEscCol129921_4176.

Organism-specific databases

EchoBASE

EB1878.

EcoGene

EG11934. aphA.

Phylogenomic databases

eggNOG

COG3700.

HOGENOM

HOG000270623.

K03788.

OMA

PEFWEKM.

ProtClustDB

PRK11009.

Enzyme and pathway databases

BioCyc

EcoCyc:APHA-MONOMER.
ECOL316407:JW4015-MONOMER.
MetaCyc:APHA-MONOMER.

BRENDA

3.1.3.2. 2026.

SABIO-RK

P0AE22.

Gene expression databases

Genevestigator

P0AE22.

Family and domain databases

Gene3D

3.40.50.1000. 1 hit.

InterPro

IPR005519. Acid_phosphat_B.
IPR023214. HAD-like_dom.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view]

Pfam

PF03767. Acid_phosphat_B. 1 hit.
[Graphical view]

PIRSF

PIRSF017818. Acid_Ptase_B. 1 hit.

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01672. AphA. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0AE22.

Entry information

Entry name

APHA_ECOLI

Accession

Primary (citable) accession number: P0AE22
Secondary accession number(s): P32697

Q57085

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents