Literature summary for 1.2.1.30 extracted from

Stolterfoht, H.; Schwendenwein, D.; Sensen, C.W.; Rudroff, F.; Winkler, M.
Four distinct types of E.C. 1.2.1.30 enzymes can catalyze the reduction of carboxylic acids to aldehydes (2017), J. Biotechnol., 257, 222-232 .

Application

Application	Comment	Organism
synthesis	the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level	Neurospora crassa
synthesis	the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level	Nocardia iowensis
synthesis	the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level	Mycobacterium marinum
synthesis	the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level	Segniliparus rotundus
synthesis	the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level	Aspergillus terreus

Cloned(Commentary)

Cloned (Comment)	Organism
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme in Escherichia coli	Nocardia iowensis
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme in Escherichia coli	Mycobacterium marinum
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme in Escherichia coli	Segniliparus rotundus
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme in Escherichia coli	Aspergillus terreus
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme with Escherichia coli phosphopantetheinyl transferase, EcPPTase, in Escherichia coli strain MG1655 RARE	Neurospora crassa

Protein Variants

Protein Variants	Comment	Organism
E337A	site-directed mutagenesis, mutant shows decreased activity compared to wild-type	Neurospora crassa
E433A	site-directed mutagenesis, mutant shows decreased activity compared to wild-type	Neurospora crassa
G432A	site-directed mutagenesis, the mutant shows activity similar to wild-type	Neurospora crassa
H237A	site-directed mutagenesis, mutant shows decreased activity compared to wild-type	Neurospora crassa
K190A	site-directed mutagenesis, the mutant shows increased activity compared to wild-type	Neurospora crassa
K848A	site-directed mutagenesis, inactive mutant	Neurospora crassa
additional information	analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively	Neurospora crassa
additional information	analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively	Nocardia iowensis
additional information	analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively	Mycobacterium marinum
additional information	analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively	Segniliparus rotundus
additional information	analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively	Aspergillus terreus
P189A	site-directed mutagenesis, the mutant shows activity similar to wild-type	Neurospora crassa
P234A	site-directed mutagenesis, the mutant shows increased activity compared to wild-type	Neurospora crassa
T186A	site-directed mutagenesis, the mutant shows activity similar to wild-type	Neurospora crassa
Y844A	site-directed mutagenesis, inactive mutant	Neurospora crassa

Metals/Ions

Metals/Ions	Comment	Organism
Mg2+	required	Neurospora crassa
Mg2+	required	Nocardia iowensis
Mg2+	required	Mycobacterium marinum
Mg2+	required	Segniliparus rotundus
Mg2+	required	Aspergillus terreus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
aromatic carboxylate + NADPH + H+ + ATP	Neurospora crassa	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Nocardia iowensis	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Mycobacterium marinum	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Segniliparus rotundus	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Aspergillus terreus	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Aspergillus terreus NIH 2624	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Mycobacterium marinum ATCC BAA-535	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Segniliparus rotundus CIP 108378	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Segniliparus rotundus ATCC BAA-972	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Segniliparus rotundus JCM 13578	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Aspergillus terreus FGSC A1156	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Segniliparus rotundus DSM 44985	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	Segniliparus rotundus CDC 1076	-	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir

Organism

Organism	UniProt	Comment	Textmining
Aspergillus terreus	Q0CRQ4	-	-
Aspergillus terreus FGSC A1156	Q0CRQ4	-	-
Aspergillus terreus NIH 2624	Q0CRQ4	-	-
Mycobacterium marinum	B2HN69	-	-
Mycobacterium marinum ATCC BAA-535	B2HN69	-	-
Neurospora crassa	-	-	-
Nocardia iowensis	Q6RKB1	-	-
Segniliparus rotundus	D6Z860	-	-
Segniliparus rotundus ATCC BAA-972	D6Z860	-	-
Segniliparus rotundus CDC 1076	D6Z860	-	-
Segniliparus rotundus CIP 108378	D6Z860	-	-
Segniliparus rotundus DSM 44985	D6Z860	-	-
Segniliparus rotundus JCM 13578	D6Z860	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
side-chain modification	The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle	Neurospora crassa
side-chain modification	The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle	Nocardia iowensis
side-chain modification	The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle	Mycobacterium marinum
side-chain modification	The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle	Segniliparus rotundus
side-chain modification	The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle	Aspergillus terreus

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and desalting gel filtration	Nocardia iowensis
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and desalting gel filtration	Mycobacterium marinum
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and desalting gel filtration	Segniliparus rotundus
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and desalting gel filtration	Aspergillus terreus
recombinant His-tagged enzyme from Escherichia coli strain MG1655 RARE by nickel affinity chromatography and desalting gel filtration	Neurospora crassa

Reaction

Reaction	Comment	Organism	Reaction ID
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP	the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol	Neurospora crassa	a
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP	the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol	Nocardia iowensis	a
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP	the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol	Mycobacterium marinum	a
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP	the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol	Segniliparus rotundus	a
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP	the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol	Aspergillus terreus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
aromatic carboxylate + NADPH + H+ + ATP	-	Neurospora crassa	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Nocardia iowensis	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Mycobacterium marinum	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Segniliparus rotundus	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Aspergillus terreus	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Aspergillus terreus NIH 2624	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Mycobacterium marinum ATCC BAA-535	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Segniliparus rotundus CIP 108378	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Segniliparus rotundus ATCC BAA-972	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Segniliparus rotundus JCM 13578	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Aspergillus terreus FGSC A1156	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Segniliparus rotundus DSM 44985	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
aromatic carboxylate + NADPH + H+ + ATP	-	Segniliparus rotundus CDC 1076	aromatic aldehyde + NADP+ + AMP + diphosphate	-	ir
cinnamate + NADPH + H+ + ATP	-	Neurospora crassa	cinnamaldehyde + NADP+ + AMP + diphosphate	-	ir
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Neurospora crassa	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Nocardia iowensis	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Mycobacterium marinum	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Segniliparus rotundus	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Aspergillus terreus	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Aspergillus terreus NIH 2624	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Mycobacterium marinum ATCC BAA-535	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Segniliparus rotundus CIP 108378	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Segniliparus rotundus ATCC BAA-972	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Segniliparus rotundus JCM 13578	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Aspergillus terreus FGSC A1156	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Segniliparus rotundus DSM 44985	?	-	-
additional information	CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes	Segniliparus rotundus CDC 1076	?	-	-

Subunits

Subunits	Comment	Organism
More	the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine	Neurospora crassa
More	the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine	Nocardia iowensis
More	the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine	Mycobacterium marinum
More	the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine	Segniliparus rotundus
More	the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine	Aspergillus terreus

Synonyms

Synonyms	Comment	Organism
CAR	-	Neurospora crassa
CAR	-	Nocardia iowensis
CAR	-	Mycobacterium marinum
CAR	-	Segniliparus rotundus
CAR	-	Aspergillus terreus
carboxylate reductase	-	Neurospora crassa
carboxylate reductase	-	Nocardia iowensis
carboxylate reductase	-	Mycobacterium marinum
carboxylate reductase	-	Segniliparus rotundus
carboxylate reductase	-	Aspergillus terreus
type I CAR	-	Mycobacterium marinum
type I CAR	-	Segniliparus rotundus
type III CAR	-	Neurospora crassa

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
28	-	assay at	Neurospora crassa

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	assay at	Neurospora crassa

Cofactor

Cofactor	Comment	Organism
ATP	-	Neurospora crassa
ATP	-	Nocardia iowensis
ATP	-	Mycobacterium marinum
ATP	-	Segniliparus rotundus
ATP	-	Aspergillus terreus
NADPH	-	Neurospora crassa
NADPH	-	Nocardia iowensis
NADPH	-	Mycobacterium marinum
NADPH	-	Segniliparus rotundus
NADPH	-	Aspergillus terreus

General Information

General Information	Comment	Organism
evolution	Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups	Neurospora crassa
evolution	Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups	Nocardia iowensis
evolution	Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups	Mycobacterium marinum
evolution	Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups	Segniliparus rotundus
evolution	Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups	Aspergillus terreus
additional information	analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity	Neurospora crassa
additional information	analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity	Nocardia iowensis
additional information	analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity	Mycobacterium marinum
additional information	analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity	Segniliparus rotundus
additional information	analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity	Aspergillus terreus
physiological function	the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle	Neurospora crassa
physiological function	the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle	Nocardia iowensis
physiological function	the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle	Mycobacterium marinum
physiological function	the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle	Segniliparus rotundus
physiological function	the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle	Aspergillus terreus