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Information on EC 2.7.1.238 - phenol phosphorylase
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2.7.1.238 phenol phosphorylaseIUBMB Comments
The enzyme, characterized from the bacterium Thauera aromatica, catalyses the first step in an anaerobic phenol degradation pathway. The enzyme, composed of three subunits, transfers the beta-phosphoryl from ATP to phenol, forming phenyl phosphate, AMP, and phosphate . During catalysis a diphosphoryl group is transferred from ATP to a histidine residue in one of the enzyme's subunits, from which phosphate is cleaved to render the reaction unidirectional. The remaining histidine phosphate subsequently serves as the actual phosphorylation agent .
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The enzyme appears in viruses and cellular organisms
Synonyms
phenylphosphate synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phenylphosphate synthase
PpsABC
phenylphosphate synthase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + phenol + H2O = AMP + phenyl phosphate + phosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP:phenol phosphotransferase (AMP-forming)
The enzyme, characterized from the bacterium Thauera aromatica, catalyses the first step in an anaerobic phenol degradation pathway. The enzyme, composed of three subunits, transfers the beta-phosphoryl from ATP to phenol, forming phenyl phosphate, AMP, and phosphate [1]. During catalysis a diphosphoryl group is transferred from ATP to a histidine residue in one of the enzyme's subunits, from which phosphate is cleaved to render the reaction unidirectional. The remaining histidine phosphate subsequently serves as the actual phosphorylation agent [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
-
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
-
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
the enzyme catalyses the first step in an anaerobic phenol degradation pathway
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
during catalysis a diphosphoryl group is transferred from ATP to a histidine residue (His569) in one of the subunits of the enzyme, from which phosphate is cleaved to render the reaction unidirectional. The remaining histidine phosphate subsequently serves as the actual phosphorylation agent
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
during catalysis a diphosphoryl group is transferred from ATP to a histidine residue (His569) in one of the subunits of the enzyme, from which phosphate is cleaved to render the reaction unidirectional. The remaining histidine phosphate subsequently serves as the actual phosphorylation agent
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
the enzyme catalyses the first step in an anaerobic phenol degradation pathway
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
-
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
-
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
the enzyme catalyses the first step in an anaerobic phenol degradation pathway
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
-
-
-
?
ATP + phenol + H2O
AMP + phenyl phosphate + phosphate
A0A2R4BQP5; A0A2R4BQP1
the enzyme catalyses the first step in an anaerobic phenol degradation pathway
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
the standard enzyme assay mixture contains 2 mM MgCl2, 2 mM MnCl2 and 2 mM KCl
Mg2+
Mn2+
-
the standard enzyme assay mixture contains 2 mM MgCl2, 2 mM MnCl2 and 2 mM KCl
Mg2+
-
the standard enzyme assay mixture contains 2 mM MgCl2, 2 mM MnCl2 and 2 mM KCl
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
A0A2R4BQP5: pPhenylphosphate synthase subunit C, A0A2R4BQP1: phenylphosphate synthase subunit A
A0A2R4BQP5; A0A2R4BQP1
UniProt
brenda
A0A2R4BQP5: phenylphosphate synthase subunit C, A0A2R4BQP1: phenylphosphate synthase subunit A
A0A2R4BQP5; A0A2R4BQP1
UniProt
brenda
A0A2R4BQP5: phenylphosphate synthase subunit C, A0A2R4BQP1: phenylphosphate synthase subunit A
A0A2R4BQP5; A0A2R4BQP1
UniProt
brenda
A0A2R4BQP5: pPhenylphosphate synthase subunit C, A0A2R4BQP1: phenylphosphate synthase subunit A
A0A2R4BQP5; A0A2R4BQP1
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
subunits A and B play an essential role in phosphorylation of phenol, which is the first step in anaerobic phenol degradation
physiological function
A0A2R4BQP5; A0A2R4BQP1
the enzyme catalyses the first step in an anaerobic phenol degradation pathway
physiological function
-
the enzyme catalyzes the first step in the anaerobic phenol degradation pathway
physiological function
-
the enzyme is involved in phenol degradation
physiological function
A0A2R4BQP5; A0A2R4BQP1
the enzyme is involved in the anaerobic metabolism of catechol
physiological function
-
the enzyme is involved in phenol degradation
-
physiological function
-
the enzyme catalyzes the first step in the anaerobic phenol degradation pathway
-
physiological function
-
subunits A and B play an essential role in phosphorylation of phenol, which is the first step in anaerobic phenol degradation
-
physiological function
-
the enzyme is involved in the anaerobic metabolism of catechol
-
physiological function
-
the enzyme catalyses the first step in an anaerobic phenol degradation pathway
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
trimer
A0A2R4BQP5; A0A2R4BQP1
the enzyme consists of three proteins: protein 1 (70 kDa) resembles the central part of classical phosphoenolpyruvate synthase which contains a conserved histidine residue. It catalyzes the exchange of free [14C]phenol and the phenol moiety of phenylphosphate but not the phosphorylation of phenol. Phosphorylation of phenol requires protein 1, MgATP, and another protein, protein 2 (40 kDa), which resembles the N-terminal part of phosphoenolpyruvate synthase. The phosphoryl group in phenylphosphate is derived from the beta-phosphate group of ATP. The free energy of ATP hydrolysis obviously favors the trapping of phenol, even at a low ambient substrate concentration. The reaction is stimulated severalfold by another protein, protein 3 (24 kDa), which contains two cystathionine-beta-synthase domains of unknown function but does not show significant overall similarity to known proteins
trimer
-
the enzyme consists of three proteins: protein 1 (70 kDa) resembles the central part of classical phosphoenolpyruvate synthase which contains a conserved histidine residue. It catalyzes the exchange of free [14C]phenol and the phenol moiety of phenylphosphate but not the phosphorylation of phenol. Phosphorylation of phenol requires protein 1, MgATP, and another protein, protein 2 (40 kDa), which resembles the N-terminal part of phosphoenolpyruvate synthase. The phosphoryl group in phenylphosphate is derived from the beta-phosphate group of ATP. The free energy of ATP hydrolysis obviously favors the trapping of phenol, even at a low ambient substrate concentration. The reaction is stimulated severalfold by another protein, protein 3 (24 kDa), which contains two cystathionine-beta-synthase domains of unknown function but does not show significant overall similarity to known proteins
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced during growth on phenol
inducible by phenol
induction during growth on phenol. No activity is measured with cell free extracts of benzoate grown cells
induction during growth on phenol. No activity is measured with cell free extracts of benzoate grown cells
-
induction during growth on phenol. No activity is measured with cell free extracts of benzoate grown cells
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xie, X.; Mller, N.
Enzymes involved in the anaerobic degradation of phenol by the sulfate-reducing bacterium Desulfatiglans anilini
BMC Microbiol.
18
93
2018
Desulfatiglans anilini, Desulfatiglans anilini DSM 4660
brenda
Ding, B.; Schmeling, S.; Fuchs, G.
Anaerobic metabolism of catechol by the denitrifying bacterium Thauera aromatica - a result of promiscuous enzymes and regulators?
J. Bacteriol.
190
1620-1630
2008
Thauera aromatica (A0A2R4BQP5 AND A0A2R4BQP1), Thauera aromatica, Thauera aromatica K172 (A0A2R4BQP5 AND A0A2R4BQP1)
brenda
Schleinitz, K.M.; Schmeling, S.; Jehmlich, N.; von Bergen, M.; Harms, H.; Kleinsteuber, S.; Vogt, C.; Fuchs, G.
Phenol degradation in the strictly anaerobic iron-reducing bacterium Geobacter metallireducens GS-15
Appl. Environ. Microbiol.
75
3912-3919
2009
Geobacter metallireducens, Geobacter metallireducens GS-15
brenda
Ahn, Y.B.; Chae, J.C.; Zylstra, G.J.; Haeggblom, M.M.
Degradation of phenol via phenylphosphate and carboxylation to 4-hydroxybenzoate by a newly isolated strain of the sulfate-reducing bacterium Desulfobacterium anilini
Appl. Environ. Microbiol.
75
4248-4253
2009
Desulfatiglans anilini (A3R4M0), Desulfatiglans anilini, Desulfatiglans anilini AK1 (A3R4M0)
brenda
Breinig, S.; Schiltz, E.; Fuchs, G.
Genes involved in anaerobic metabolism of phenol in the bacterium Thauera aromatica
J. Bacteriol.
182
5849-5863
2000
Thauera aromatica (A0A2R4BQP5 AND A0A2R4BQP1), Thauera aromatica, Thauera aromatica K172 (A0A2R4BQP5 AND A0A2R4BQP1)
brenda
Schmeling, S.; Narmandakh, A.; Schmitt, O.; Gadon, N.; Schuehle, K.; Fuchs, G.
Phenylphosphate synthase a new phosphotransferase catalyzing the first step in anaerobic phenol metabolism in Thauera aromatica
J. Bacteriol.
186
8044-8057
2004
Thauera aromatica (A0A2R4BQP5 AND A0A2R4BQP1), Thauera aromatica, Thauera aromatica K172 (A0A2R4BQP5 AND A0A2R4BQP1)
brenda
Narmandakh, A.; Gadon, N.; Drepper, F.; Knapp, B.; Haehnel, W.; Fuchs, G.
Phosphorylation of phenol by phenylphosphate synthase role of histidine phosphate in catalysis
J. Bacteriol.
188
7815-7822
2006
Thauera aromatica (A0A2R4BQP5 AND A0A2R4BQP1), Thauera aromatica, Thauera aromatica DSM 6984 (A0A2R4BQP5 AND A0A2R4BQP1)
brenda
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Release 2023.1 (January 2023)
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