Any feedback?
Information on EC 6.2.1.66 - glyine---[glycyl-carrier protein] ligase
for references in articles please use BRENDA:EC6.2.1.66Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
6.2.1.66 glyine---[glycyl-carrier protein] ligaseIUBMB Comments
The adenylation domain of the enzyme catalyses the activation of glycine to (glycyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein (as in the case of DhbF in bacillibactin biosynthesis), or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
Specify your search results
Word Map
- 6.2.1.66
- polyketide
-
synthetases
-
siderophore
-
nrpss
-
lipopeptide
-
thioesterase
-
peptidyl
-
depsipeptide
-
phosphopantetheinylated
-
nonproteinogenic
-
multimodular
-
roseosporus
-
ketosynthase
-
cyclodepsipeptide
- 2,3-dihydroxybenzoate
- enterobactin
-
cereulide
-
trimodular
-
nrps-pk
-
marfey
-
pks-nrps
- halogenase
-
tyrocidine
-
a-domains
-
daptomycin
- mbth
-
nrps-like
-
yersiniabactin
-
thiazoline
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
holo-[glycyl-carrier protein]
=
+
+
glycyl-[glycyl-carrier protein]
Synonyms
nonribosomal peptide synthetase, dimodular nrps, dimodular nonribosomal peptide synthetase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dhbF
dimodular nonribosomal peptide synthase
dimodular nonribosomal peptide synthetase
dimodular NRPS
nonribosomal peptide synthetase
sfmB
dhbF
-
-
-
-
sfmB
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(glycyl)adenylate + holo-[glycyl-carrier protein] = AMP + glycyl-[glycyl-carrier protein]
(1b)
-
-
-
ATP + glycine + holo-[glycyl-carrier protein] = AMP + diphosphate + glycyl-[glycyl-carrier protein]
overall reaction
-
-
-
ATP + glycine = diphosphate + (glycyl)adenylate
(1a)
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
glycine:[glycyl-carrier protein] ligase (AMP-forming)
The adenylation domain of the enzyme catalyses the activation of glycine to (glycyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein (as in the case of DhbF in bacillibactin biosynthesis), or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
(glycyl)adenylate + holo-[glycyl-carrier protein]
AMP + glycyl-[glycyl-carrier protein]
-
-
-
ir
(glycyl)adenylate + holo-[glycyl-carrier protein]
AMP + glycyl-[glycyl-carrier protein]
-
-
-
-
ir
(glycyl)adenylate + holo-[glycyl-carrier protein]
AMP + glycyl-[glycyl-carrier protein]
-
-
-
ir
(glycyl)adenylate + holo-[glycyl-carrier protein]
AMP + glycyl-[glycyl-carrier protein]
-
-
-
ir
(glycyl)adenylate + holo-[glycyl-carrier protein]
AMP + glycyl-[glycyl-carrier protein]
-
-
-
ir
ATP + glycine
diphosphate + (glycyl)adenylate
-
-
-
ir
ATP + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
-
-
-
ir
ATP + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
-
-
-
-
ir
ATP + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
-
-
-
ir
ATP + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
-
-
-
ir
ATP + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
-
-
-
ir
additional information
?
-
substrate selectivity of the recombinant DhbF. Comparative mass spectrometric analysis of culture extracts from both the wild-type DhbF and the dhbF knockout mutant leads to the identification of a cyclic trimeric ester of DHB-glycine-threonine. Enzyme activity assay by ATP-diphosphate exchange reaction. For the DhbF1-A-PCP construct, a low but specific glycine-dependent ATP-diphosphate exchange is observed. For the second module, DhbF2-A-PCP, a highly specific ATP-diphosphate exchange dependent on L-threonine is observed. D-Threonine is not recognized as a substrate, whereas the stereoisomeric L-allo-Thr covers 47% activity
-
-
-
additional information
?
-
-
substrate selectivity of the recombinant DhbF. Comparative mass spectrometric analysis of culture extracts from both the wild-type DhbF and the dhbF knockout mutant leads to the identification of a cyclic trimeric ester of DHB-glycine-threonine. Enzyme activity assay by ATP-diphosphate exchange reaction. For the DhbF1-A-PCP construct, a low but specific glycine-dependent ATP-diphosphate exchange is observed. For the second module, DhbF2-A-PCP, a highly specific ATP-diphosphate exchange dependent on L-threonine is observed. D-Threonine is not recognized as a substrate, whereas the stereoisomeric L-allo-Thr covers 47% activity
-
-
-
additional information
?
-
substrate selectivity of the recombinant DhbF. Comparative mass spectrometric analysis of culture extracts from both the wild-type DhbF and the dhbF knockout mutant leads to the identification of a cyclic trimeric ester of DHB-glycine-threonine. Enzyme activity assay by ATP-diphosphate exchange reaction. For the DhbF1-A-PCP construct, a low but specific glycine-dependent ATP-diphosphate exchange is observed. For the second module, DhbF2-A-PCP, a highly specific ATP-diphosphate exchange dependent on L-threonine is observed. D-Threonine is not recognized as a substrate, whereas the stereoisomeric L-allo-Thr covers 47% activity
-
-
-
additional information
?
-
recombinant SfmB (C2-A2-PCP2) shows exclusive activities with Gly, determination of substrate specificities of SfmB by utilizing amino acid-dependent ATP-diphosphate exchange assay
-
-
-
additional information
?
-
recombinant SfmB (C2-A2-PCP2) shows exclusive activities with Gly, determination of substrate specificities of SfmB by utilizing amino acid-dependent ATP-diphosphate exchange assay
-
-
-
additional information
?
-
-
recombinant SfmB (C2-A2-PCP2) shows exclusive activities with Gly, determination of substrate specificities of SfmB by utilizing amino acid-dependent ATP-diphosphate exchange assay
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
(glycyl)adenylate + holo-[glycyl-carrier protein]
AMP + glycyl-[glycyl-carrier protein]
-
-
-
ir
(glycyl)adenylate + holo-[glycyl-carrier protein]
AMP + glycyl-[glycyl-carrier protein]
-
-
-
-
ir
(glycyl)adenylate + holo-[glycyl-carrier protein]
AMP + glycyl-[glycyl-carrier protein]
-
-
-
ir
(glycyl)adenylate + holo-[glycyl-carrier protein]
AMP + glycyl-[glycyl-carrier protein]
-
-
-
ir
(glycyl)adenylate + holo-[glycyl-carrier protein]
AMP + glycyl-[glycyl-carrier protein]
-
-
-
ir
ATP + glycine
diphosphate + (glycyl)adenylate
-
-
-
ir
ATP + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
-
-
-
ir
ATP + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
-
-
-
-
ir
ATP + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
-
-
-
ir
ATP + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
-
-
-
ir
ATP + glycine + holo-[glycyl-carrier protein]
AMP + diphosphate + glycyl-[glycyl-carrier protein]
-
-
-
ir
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Bacterial Infections
Marine macroalgae-associated heterotrophic Firmicutes and Gamma-proteobacteria: prospective anti-infective agents against multidrug resistant pathogens.
Infections
Total Biosynthesis and Diverse Applications of the Nonribosomal Peptide-Polyketide Siderophore Yersiniabactin.
Scabies
Structure and biosynthesis of scabichelin, a novel tris-hydroxamate siderophore produced by the plant pathogen Streptomyces scabies 87.22.
Tuberculosis
Function of MbtH homologs in nonribosomal peptide biosynthesis and applications in secondary metabolite discovery.
Tuberculosis
Mycobacterium tuberculosis SigM positively regulates Esx secreted protein and nonribosomal peptide synthetase genes and down regulates virulence-associated surface lipid synthesis.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
disruption of chromosomal dhb genes results in 2,3-dihydroxybenzoate (DHB) deficiency
malfunction
the sfmB mutant strain TL2003 completely loses its ability to produce SFM-A, which is restored by expressing sfmB in trans, confirming the essential role of this NRPS system for SFM-A biosynthesis
malfunction
-
disruption of chromosomal dhb genes results in 2,3-dihydroxybenzoate (DHB) deficiency
-
malfunction
-
the sfmB mutant strain TL2003 completely loses its ability to produce SFM-A, which is restored by expressing sfmB in trans, confirming the essential role of this NRPS system for SFM-A biosynthesis
-
metabolism
proposed biosynthetic pathway for saframycin A involving genes sfmA, sfmB, and sfmC, overview
metabolism
-
proposed biosynthetic pathway for saframycin A involving genes sfmA, sfmB, and sfmC, overview
-
physiological function
Bacillus subtilis produces the catecholic siderophore itoic acid (2,3-dihydroxybenzoate (DHB)-glycine) in response to iron deprivation. According to the corrected sequence, dhbF encodes a dimodular instead of a monomodular nonribosomal peptide synthetase. DhbF specifically adenylates threonine and, to a lesser extent, glycine and that covalently loads both amino acids onto their corresponding peptidyl carrier domains. The function of the terminal thioesterase domain (DhbF-Te) is to catalyze the intermolecular condensation of three DHB-Gly-Thr units and to release bacillibactin by intramolecular condensation. Mass spectrometric analysis, overview. Model for the assembly of bacillibactin
physiological function
enzyme DhbF is involved in the addition of glycine to the siderophore 2,3-dihydroxybenzoate (DHB). Under iron-limiting conditions, Bacillus subtilis produces DHB to acquire extracellular iron
physiological function
the enzyme is involved in the synthesis of saframycin A (SFM-A) by Streptomyces lavendulae strain NRRL 11002. The compound belongs to the tetrahydroisoquinoline family of antibiotics. The backbone of SFM-A is derived from one Ala, one Gly, and two Tyr residues, suggesting that it is of tetrapeptide origin. SfmA, SfmB, and SfmC constitute an NRPS system
physiological function
-
Bacillus subtilis produces the catecholic siderophore itoic acid (2,3-dihydroxybenzoate (DHB)-glycine) in response to iron deprivation. According to the corrected sequence, dhbF encodes a dimodular instead of a monomodular nonribosomal peptide synthetase. DhbF specifically adenylates threonine and, to a lesser extent, glycine and that covalently loads both amino acids onto their corresponding peptidyl carrier domains. The function of the terminal thioesterase domain (DhbF-Te) is to catalyze the intermolecular condensation of three DHB-Gly-Thr units and to release bacillibactin by intramolecular condensation. Mass spectrometric analysis, overview. Model for the assembly of bacillibactin
-
physiological function
-
enzyme DhbF is involved in the addition of glycine to the siderophore 2,3-dihydroxybenzoate (DHB). Under iron-limiting conditions, Bacillus subtilis produces DHB to acquire extracellular iron
-
physiological function
-
the enzyme is involved in the synthesis of saframycin A (SFM-A) by Streptomyces lavendulae strain NRRL 11002. The compound belongs to the tetrahydroisoquinoline family of antibiotics. The backbone of SFM-A is derived from one Ala, one Gly, and two Tyr residues, suggesting that it is of tetrapeptide origin. SfmA, SfmB, and SfmC constitute an NRPS system
-
additional information
the biosynthetic gene cluster for SFM-A is cloned and localized to a 62-kb contiguous DNA region. Sequence analysis revealed 30 genes that constitute the SFM-A gene cluster, encoding an unusual nonribosomal peptide synthetase (NRPS) system and tailoring enzymes and regulatory and resistance proteins. The results of substrate prediction and in vitro characterization of the adenylation specificities of this NRPS system support the hypothesis that the last module acts in an iterative manner to form a tetrapeptidyl intermediate and that the co-linearity rule does not apply
additional information
-
the biosynthetic gene cluster for SFM-A is cloned and localized to a 62-kb contiguous DNA region. Sequence analysis revealed 30 genes that constitute the SFM-A gene cluster, encoding an unusual nonribosomal peptide synthetase (NRPS) system and tailoring enzymes and regulatory and resistance proteins. The results of substrate prediction and in vitro characterization of the adenylation specificities of this NRPS system support the hypothesis that the last module acts in an iterative manner to form a tetrapeptidyl intermediate and that the co-linearity rule does not apply
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
generation of a dhbF gene disruption mutant generated from Bacillus subtilis strain ATCC 21332, integration and the double crossover event in the resulting Bacillus subtilis strain JJM405
additional information
-
generation of a dhbF gene disruption mutant generated from Bacillus subtilis strain ATCC 21332, integration and the double crossover event in the resulting Bacillus subtilis strain JJM405
additional information
-
generation of a dhbF gene disruption mutant generated from Bacillus subtilis strain ATCC 21332, integration and the double crossover event in the resulting Bacillus subtilis strain JJM405
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme DhbF, and separate DhbF modules DhbF1-A-PCP and DhbF2-A-PCP, from Escherichia coli strain BL21 by nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dhbF, DNA and amino acid sequence determination and analysis. By inspecting the DNA sequences of the genes dhbE, dhbB, and dhbF as annotated by the Bacillus subtilis genome project to encode the synthetase complex for the siderophore assembly, various sequence errors within the dhbF gene are predicted and confirmed by re-sequencing. According to the corrected sequence, dhbF encodes a dimodular instead of a monomodular nonribosomal peptide synthetase, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21, the separate DhbF modules DhbF1-A-PCP and DhbF2-A-PCP are also produced as individual proteins
gene dhbF, genetic organization of the Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes, cloning from a Bacillus subtilis YAC library, DNA and amino acid sequence determination and analysis, the dhb genes are located near 291° on the Bacillus subtilis chromosome
the biosynthetic gene cluster for SFM-A is cloned and localized to a 62-kb contiguous DNA region. Sequence analysis reveals 30 genes that constitute the SFM-A gene cluster, encoding an unusual nonribosomal peptide synthetase (NRPS) system and tailoring enzymes and regulatory and resistance proteins. Three NRPS genes, sfmA, sfmB and sfmC, are identified within the sfm cluster. Cloning of gene sfmB, part of the SFM-A gene cluster, DNA and amino acid sequence determination and analysis, genetic organization, recombinant expression in Pseudomonas fluorescens
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rowland, B.; Grossman, T.; Osburne, M.; Taber, H.
Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes
Gene
178
119-123
1996
Bacillus subtilis (P45745), Bacillus subtilis 168 (P45745)
brenda
Li, L.; Deng, W.; Song, J.; Ding, W.; Zhao, Q.; Peng, C.; Song, W.; Tang, G.; Liu, W.
Characterization of the saframycin A gene cluster from Streptomyces lavendulae NRRL 11002 revealing a nonribosomal peptide synthetase system for assembling the unusual tetrapeptidyl skeleton in an iterative manner
J. Bacteriol.
190
251-263
2008
Streptomyces lavendulae (B0CN26), Streptomyces lavendulae NRRL 11002 (B0CN26), Streptomyces lavendulae NRRL 11002
brenda
May, J.; Wendrich, T.; Marahiel, M.
The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin
J. Biol. Chem.
276
7209-7217
2001
Bacillus subtilis (P45745), Bacillus subtilis, Bacillus subtilis 168 (P45745)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 6.2.1.66)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
