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Information on EC 6.2.1.50 - 4-hydroxybenzoate adenylyltransferase FadD22 and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WQ61

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.50 4-hydroxybenzoate adenylyltransferase FadD22
IUBMB Comments
This mycobacterial enzyme participates in the biosynthesis of phenolphthiocerols. Following the substrate's activation by adenylation, it is transferred to an acyl-carrier protein domain within the enzyme, from which it is transferred to EC 2.3.1.261, 4-hydroxyphenylalkanoate synthase.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WQ61
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Mycobacteriaceae
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
+
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holo-[4-hydroxyphenylalkanoate synthase]
=
+
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4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase]
Synonyms
fadd22, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
p-hydroxybenzoic acid-AMP ligase
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4-hydroxybenzoate adenylas
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fadD22
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxybenzoate:holo-[4-hydroxyphenylalkanoate synthase] ligase (AMP-forming)
This mycobacterial enzyme participates in the biosynthesis of phenolphthiocerols. Following the substrate's activation by adenylation, it is transferred to an acyl-carrier protein domain within the enzyme, from which it is transferred to EC 2.3.1.261, 4-hydroxyphenylalkanoate synthase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxybenzoyl-adenylate + holo-[4-hydroxyphenylalkanoate synthase]
AMP + 4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase]
show the reaction diagram
-
-
-
?
ATP + 4-hydroxybenzoate
4-hydroxybenzoyl-adenylate + diphosphate
show the reaction diagram
-
-
-
?
ATP + 4-hydroxybenzoate + holo-[4-hydroxyphenylalkanoate synthase]
AMP + diphosphate + 4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase]
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxybenzoyl-adenylate + holo-[4-hydroxyphenylalkanoate synthase]
AMP + 4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase]
show the reaction diagram
-
-
-
?
ATP + 4-hydroxybenzoate
4-hydroxybenzoyl-adenylate + diphosphate
show the reaction diagram
-
-
-
?
ATP + 4-hydroxybenzoate + holo-[4-hydroxyphenylalkanoate synthase]
AMP + diphosphate + 4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase]
show the reaction diagram
-
-
-
?
additional information
?
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
disruption of FadD22 abolishes the production of its species-specific phenolic glycolipid
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Simeone, R; Lger, M.; Constant, P.; Malaga, W.; Marrakchi, H.; Daff, M.; Guilhot, C.; Chalut, C.
Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis
FEBS J.
277
2715-2725
2010
Mycobacterium tuberculosis (P9WQ61), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WQ61)
Manually annotated by BRENDA team