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MetaCyc Enzyme: acid phosphatase / phosphotransferase

Gene: aphA Accession Numbers: EG11934 (MetaCyc), b4055, ECK4047

Synonyms: yjbP, hobH

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of acid phosphatase / phosphotransferase = [AphA]4
         AphA monomer = AphA

Summary:
aphA encodes a periplasmic phosphatase/phosphotransferase that has optimal activity at acidic pH.

The purified enzyme is able to dephosphorylate 5' and 3' mononucleotides, 2-deoxy 5' nucleotides, phenylphosphate, glycerol-2-phosphate, ribose-5-phosphate, O-phospho-L-amino acids (O-phospho-L-serine, O-phospho-L-threonine and O-phospho-L-tyrosine) and phytic acid. No activity was observed on ATP, phosphodiesters, glycerol-1-phosphate, glucose-1-phosphate or glucose-6-phosphate. Purified AphA has phosphotransferase activity, catalysing phosphate transfer from p-nitrophenyl phosphate (pNPP) to adenosine or uridine [Thaller97]

The purified enzyme is active on 3' mononucleotides, 3' monodeoxynucleotides, 5' mononucleotides and 5' monodeoxynucleotides. The purifed enzyme is not active on 3', 5'-cyclic AMP, ADP, ATP, NADH or GTP and shows low activity with sugar phosphates and β glycerol phosphate The purified enzyme does not have any phosphomutase activity but can act as a phosphotransferase [Passariello06].

AphA activity is inhibited by EDTA suggesting that it is a metallo-protein [Thaller97, Passariello06].

Purified AphA is a homotetramer [Thaller97]

AphA is found at high abundance in vivo [Link97].

HobH: hemimethylated origin binding [Herrick94]

Locations: periplasmic space

Map Position: [4,267,437 -> 4,268,150]

Molecular Weight of Polypeptide: 26.104 kD (from nucleotide sequence)

Molecular Weight of Multimer: 101.0 kD (experimental) [Thaller97]

pI: 6.85 [Han13]

Unification Links: ASAP:ABE-0013283 , EchoBASE:EB1878 , EcoGene:EG11934 , EcoliWiki:b4055 , Mint:MINT-1294190 , ModBase:P0AE22 , OU-Microarray:b4055 , PortEco:aphA , PR:PRO_000022108 , Pride:P0AE22 , Protein Model Portal:P0AE22 , RefSeq:NP_418479 , RegulonDB:EG11934 , SMR:P0AE22 , String:511145.b4055 , Swiss-Model:P0AE22 , UniProt:P0AE22

Relationship Links: InterPro:IN-FAMILY:IPR005519 , InterPro:IN-FAMILY:IPR010025 , InterPro:IN-FAMILY:IPR023214 , PDB:Structure:1N8N , PDB:Structure:1N9K , PDB:Structure:1RMQ , PDB:Structure:1RMT , PDB:Structure:1RMY , PDB:Structure:2B82 , PDB:Structure:2B8J , PDB:Structure:2G1A , PDB:Structure:2HEG , PDB:Structure:2HF7 , PDB:Structure:3CZ4 , Pfam:IN-FAMILY:PF03767

Gene-Reaction Schematic: ?

Instance reaction of [a phosphate monoester + H2O ↔ an alcohol + phosphate] (3.1.3.2):
i1: ethylphosphate + H2O → ethanol + phosphate (3.1.3.1)

Instance reactions of [a nucleoside 3'-phosphate + H2O → a ribonucleoside + phosphate] (3.1.3.6):
i13: adenosine 3'-monophosphate + H2O → adenosine + phosphate (3.1.3.6)

i14: guanosine 3'-monophosphate + H2O → guanosine + phosphate (3.1.3.6)

i15: cytidine-3'-monophosphate + H2O → cytidine + phosphate (3.1.3.6)

i16: uridine 3'-monophosphate + H2O → uridine + phosphate (3.1.3.6)

Instance reactions of [a 2'-deoxyribonucleoside 3'-monophosphate[periplasmic space] + H2O[periplasmic space] → a 2'-deoxynucleoside[periplasmic space] + phosphate[periplasmic space]] (3.1.3.34):
i17: thymidine 3'-monophosphate + H2O → thymidine + phosphate (3.1.3.34)

i18: 2'-deoxyguanosine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] → 2'-deoxyguanosine[periplasmic space] + phosphate[periplasmic space] (3.1.3.34)

i19: 2'-deoxyadenosine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] → 2'-deoxyadenosine[periplasmic space] + phosphate[periplasmic space] (3.1.3.34)

i20: 2'-deoxycytidine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] → 2'-deoxycytidine[periplasmic space] + phosphate[periplasmic space] (3.1.3.34)

i21: 2'-deoxyuridine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] → 2'-deoxyuridine[periplasmic space] + phosphate[periplasmic space] (3.1.3.34)

Instance reactions of [a nucleoside 5'-monophosphate[periplasmic space] + H2O[periplasmic space] → a nucleoside[periplasmic space] + phosphate[periplasmic space]] (no EC#):
i2: dCMP + H2O → 2'-deoxycytidine + phosphate (3.1.3.89)

i3: dUMP + H2O → 2'-deoxyuridine + phosphate (3.1.3.89)

i4: dTMP + H2O → thymidine + phosphate (3.1.3.89)

i5: dAMP + H2O → 2'-deoxyadenosine + phosphate (3.1.3.89)

i6: dGMP + H2O → 2'-deoxyguanosine + phosphate (3.1.3.89)

i7: GMP + H2O → guanosine + phosphate (3.1.3.5)

i8: CMP + H2O → cytidine + phosphate (3.1.3.91)

i9: IMP + H2O → inosine + phosphate (3.1.3.5)

i10: UMP + H2O → uridine + phosphate (3.1.3.5)

i11: XMP + H2O → xanthosine + phosphate (3.1.3.5)

i12: AMP[periplasmic space] + H2O[periplasmic space] → adenosine[periplasmic space] + phosphate[periplasmic space] (3.1.3.5)

GO Terms:

Biological Process: GO:0016311 - dephosphorylation Inferred by computational analysis Inferred from experiment [Thaller97, Passariello06, GOA01, GOA01a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0003993 - acid phosphatase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Thaller97, Passariello06]
GO:0004647 - phosphoserine phosphatase activity Inferred from experiment [Thaller97]
GO:0048037 - cofactor binding Inferred from experiment [Thaller97, Calderone04]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment Inferred by computational analysis [GOA01a, DiazMejia09, Han13, Rossolini94]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: metabolism central intermediary metabolism nucleotide and nucleoside conversions

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: acid phosphatase / phosphotransferase

Synonyms: class B acid phosphatase/phosphotransferase, acid phosphatase, non-specific acid phosphatase, NAP, acid phosphomonoesterase, phosphomonoesterase, glycerophosphatase, orthophosphoric-monoester phosphohydrolase (acid optimum)

EC Number: 3.1.3.2

a phosphate monoester[periplasmic space] + H2O[periplasmic space] <=> an alcohol[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Alternative Substrates for a phosphate monoester: glycerol 2-phosphate [Thaller97 ] , 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate [Thaller97 ]

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Cofactors or Prosthetic Groups: Mg2+ [Comment 1]

Activators (Unknown Mechanism): ethanol [Thaller97]

Inhibitors (Unknown Mechanism): guanosine [Thaller97] , a nucleoside [Thaller97] , Ca2+ [Thaller97] , phosphate [Thaller97] , uridine [Thaller97] , EDTA [Thaller97]

Primary Physiological Regulators of Enzyme Activity: Ca2+ , phosphate , uridine

pH(opt): 6 [Rossolini94]


Enzymatic reaction of: nucleoside monophosphate phosphatase (acid phosphatase / phosphotransferase)

a nucleoside 5'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> a nucleoside[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: adenosine nucleotides degradation II , urate biosynthesis/inosine 5'-phosphate degradation , purine nucleotides degradation II (aerobic) , guanosine nucleotides degradation III

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: nucleoside 5'-monophosphate phosphatase (acid phosphatase / phosphotransferase)

EC Number: 3.1.3.5

a ribonucleoside 5'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> a ribonucleoside[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: adenosine nucleotides degradation II , urate biosynthesis/inosine 5'-phosphate degradation , purine nucleotides degradation II (aerobic) , guanosine nucleotides degradation III

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: nucleoside 3'-monophosphate phosphatase (acid phosphatase / phosphotransferase)

EC Number: 3.1.3.6

a nucleoside 3'-phosphate[periplasmic space] + H2O[periplasmic space] <=> a ribonucleoside[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 2'-deoxyribonucleoside 5'-monophosphate phosphatase (acid phosphatase / phosphotransferase)

EC Number: 3.1.3.89

a 2'-deoxyribonucleoside 5'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> a 2'-deoxynucleoside[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 2'-deoxyribonucleoside 3'-monophosphate phosphatase (acid phosphatase / phosphotransferase)

EC Number: 3.1.3.34

a 2'-deoxyribonucleoside 3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> a 2'-deoxynucleoside[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 2'-deoxycytidine 3'-monophosphate phosphatase (acid phosphatase / phosphotransferase)

EC Number: 3.1.3.34

2'-deoxycytidine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> 2'-deoxycytidine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Kinetic Parameters:

Substrate
Km (μM)
Citations
2'-deoxycytidine 3'-monophosphate
1.3
[Passariello06]


Enzymatic reaction of: 2'-deoxyguanosine 3'-monophosphate phosphatase (acid phosphatase / phosphotransferase)

EC Number: 3.1.3.34

2'-deoxyguanosine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> 2'-deoxyguanosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Kinetic Parameters:

Substrate
Km (μM)
Citations
2'-deoxyguanosine 3'-monophosphate
1.6
[Passariello06]


Enzymatic reaction of: 2'-deoxyuridine 3'-monophosphate phosphatase (acid phosphatase / phosphotransferase)

EC Number: 3.1.3.34

2'-deoxyuridine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> 2'-deoxyuridine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Kinetic Parameters:

Substrate
Km (μM)
Citations
2'-deoxyuridine 3'-monophosphate
0.9
[Passariello06]


Enzymatic reaction of: 2'-deoxyadenosine 3'-monophosphate phosphatase (acid phosphatase / phosphotransferase)

EC Number: 3.1.3.34

2'-deoxyadenosine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> 2'-deoxyadenosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Kinetic Parameters:

Substrate
Km (μM)
Citations
2'-deoxyadenosine 3'-monophosphate
1.5
[Passariello06]


Enzymatic reaction of: L-threonine O-3-phosphate phosphatase (acid phosphatase / phosphotransferase)

EC Number: 3.1.3.-

L-threonine 3-O-phosphate[periplasmic space] + H2O[periplasmic space] <=> L-threonine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 3-phosphoserine phosphatase (acid phosphatase / phosphotransferase)

3-phospho-L-serine[periplasmic space] + H2O[periplasmic space] <=> L-serine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: O-phospho-L-tyrosine phosphatase (acid phosphatase / phosphotransferase)

O-phospho-L-tyrosine[periplasmic space] + H2O[periplasmic space] <=> L-tyrosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 25
[Link97, UniProt11]
UniProt: Or 23.
Chain 26 -> 237
[UniProt09]
UniProt: Class B acid phosphatase;
Active-Site 69
[UniProt12]
UniProt: Nucleophile.
Metal-Binding-Site 69
[UniProt, 2010]
UniProt: Magnesium;
Active-Site 71
[UniProt12]
UniProt: Proton donor.
Metal-Binding-Site 71
[UniProt, 2010]
UniProt: Magnesium; via carbonyl oxygen;
Protein-Segment 137 -> 138
[UniProt12]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Amino-Acid-Sites-That-Bind 177
[UniProt12]
UniProt: Substrate.
Metal-Binding-Site 192
[UniProt, 2010]
UniProt: Magnesium;

History:
10/20/97 Gene b4055 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11934; confirmed by SwissProt match.


References

Calderone04: Calderone V, Forleo C, Benvenuti M, Cristina Thaller M, Maria Rossolini G, Mangani S (2004). "The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold." J Mol Biol 335(3);761-73. PMID: 14687572

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Han13: Han MJ, Kim JY, Kim JA (2013). "Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains." J Biosci Bioeng. PMID: 24140104

Herrick94: Herrick J, Kern R, Guha S, Landoulsi A, Fayet O, Malki A, Kohiyama M (1994). "Parental strand recognition of the DNA replication origin by the outer membrane in Escherichia coli." EMBO J 13(19);4695-703. PMID: 7925311

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

Passariello06: Passariello C, Forleo C, Micheli V, Schippa S, Leone R, Mangani S, Thaller MC, Rossolini GM (2006). "Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655." Biochim Biophys Acta 1764(1);13-9. PMID: 16297670

Rossolini94: Rossolini GM, Thaller MC, Pezzi R, Satta G (1994). "Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component." FEMS Microbiol Lett 118(1-2);167-73. PMID: 8013875

Thaller97: Thaller MC, Schippa S, Bonci A, Cresti S, Rossolini GM (1997). "Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product." FEMS Microbiol Lett 1997;146(2);191-8. PMID: 9011040

UniProt, 2010: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt12: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, biocyc13.