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Information on EC 6.2.1.67 - L-alanine---[L-alanyl-carrier protein] ligase
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EC Tree
6.2.1.67 L-alanine---[L-alanyl-carrier protein] ligaseIUBMB Comments
The adenylation domain of the enzyme catalyses the activation of L-alanine to (L-alanyl)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, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
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Word Map
- 6.2.1.67
- polyketide
-
synthetases
-
siderophore
-
lipopeptide
-
nrpss
- halogenase
-
phosphopantetheinyl
-
ketosynthase
- pptases
-
pyoverdine
-
xenorhabdus
-
roseosporus
-
nrps-like
-
indigoidine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
holo-[L-alanyl-carrier protein]
=
+
+
L-alanyl-[L-alanyl-carrier protein]
Synonyms
non-ribosomal peptide synthetase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alanine thioester-forming activity
ambB
non-ribosomal peptide synthetase
nonribosomal peptide synthetase
peptide synthetase PhsB
phosphinothricin tripeptide synthetase
phosphinothricin tripeptide synthetase III
phsB
PhsC
sfmA
additional information
ambB
-
-
-
-
phosphinothricin tripeptide synthetase III
Q5IW58, Q5IW60
UniProt
phosphinothricin tripeptide synthetase III
Q5IW58, Q5IW60
UniProt
-
phsB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein] = AMP + L-alanyl-[L-alanyl-carrier protein]
(1b)
-
-
-
ATP + L-alanine + holo-[L-alanyl-carrier protein] = AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
overall reaction
-
-
-
ATP + L-alanine = diphosphate + (L-alanyl)adenylate
(1a)
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-alanine:[L-alanyl-carrier protein] ligase (AMP-forming)
The adenylation domain of the enzyme catalyses the activation of L-alanine to (L-alanyl)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, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
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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
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
Q5IW58, Q5IW60
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
Q5IW58, Q5IW60
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
Q5IW58, Q5IW60
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
Q5IW58, Q5IW60
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
Q5IW58, Q5IW60
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
Q5IW58, Q5IW60
-
-
-
ir
additional information
?
-
enzyme AmbE (L-glutamate-[L-glutamyl-carrier protein] ligase EC 6.2.1.68) is also active with L-alanine instead of L-glutamate, but only in presence of the L-alanine-[L-alanyl-carrier protein] ligase AmbB, AmbB-dependent loading of L-Ala onto the T2 domain of AmbE, overview. Analysis of enzyme peptide fragment binding with substrate, peptide analysis by mass spectrometry, overview
-
-
-
additional information
?
-
enzyme AmbE (L-glutamate-[L-glutamyl-carrier protein] ligase EC 6.2.1.68) is also active with L-alanine instead of L-glutamate, but only in presence of the L-alanine-[L-alanyl-carrier protein] ligase AmbB, AmbB-dependent loading of L-Ala onto the T2 domain of AmbE, overview. Analysis of enzyme peptide fragment binding with substrate, peptide analysis by mass spectrometry, overview
-
-
-
additional information
?
-
enzyme AmbE (L-glutamate-[L-glutamyl-carrier protein] ligase EC 6.2.1.68) is also active with L-alanine instead of L-glutamate, but only in presence of the L-alanine-[L-alanyl-carrier protein] ligase AmbB, AmbB-dependent loading of L-Ala onto the T2 domain of AmbE, overview. Analysis of enzyme peptide fragment binding with substrate, peptide analysis by mass spectrometry, overview
-
-
-
additional information
?
-
enzyme AmbE (L-glutamate-[L-glutamyl-carrier protein] ligase EC 6.2.1.68) is also active with L-alanine instead of L-glutamate, but only in presence of the L-alanine-[L-alanyl-carrier protein] ligase AmbB, AmbB-dependent loading of L-Ala onto the T2 domain of AmbE, overview. Analysis of enzyme peptide fragment binding with substrate, peptide analysis by mass spectrometry, overview
-
-
-
additional information
?
-
enzyme AmbE (L-glutamate-[L-glutamyl-carrier protein] ligase EC 6.2.1.68) is also active with L-alanine instead of L-glutamate, but only in presence of the L-alanine-[L-alanyl-carrier protein] ligase AmbB, AmbB-dependent loading of L-Ala onto the T2 domain of AmbE, overview. Analysis of enzyme peptide fragment binding with substrate, peptide analysis by mass spectrometry, overview
-
-
-
additional information
?
-
enzyme AmbE (L-glutamate-[L-glutamyl-carrier protein] ligase EC 6.2.1.68) is also active with L-alanine instead of L-glutamate, but only in presence of the L-alanine-[L-alanyl-carrier protein] ligase AmbB, AmbB-dependent loading of L-Ala onto the T2 domain of AmbE, overview. Analysis of enzyme peptide fragment binding with substrate, peptide analysis by mass spectrometry, overview
-
-
-
additional information
?
-
enzyme AmbE (L-glutamate-[L-glutamyl-carrier protein] ligase EC 6.2.1.68) is also active with L-alanine instead of L-glutamate, but only in presence of the L-alanine-[L-alanyl-carrier protein] ligase AmbB, AmbB-dependent loading of L-Ala onto the T2 domain of AmbE, overview. Analysis of enzyme peptide fragment binding with substrate, peptide analysis by mass spectrometry, overview
-
-
-
additional information
?
-
enzyme AmbE (L-glutamate-[L-glutamyl-carrier protein] ligase EC 6.2.1.68) is also active with L-alanine instead of L-glutamate, but only in presence of the L-alanine-[L-alanyl-carrier protein] ligase AmbB, AmbB-dependent loading of L-Ala onto the T2 domain of AmbE, overview. Analysis of enzyme peptide fragment binding with substrate, peptide analysis by mass spectrometry, overview
-
-
-
additional information
?
-
recombinant SfmA module (C1-A1-PCP1) shows exclusive activities with L-Ala, determination of substrate specificities of SfmA by utilizing amino acid-dependent ATP-diphosphate exchange assay
-
-
-
additional information
?
-
recombinant SfmA module (C1-A1-PCP1) shows exclusive activities with L-Ala, determination of substrate specificities of SfmA by utilizing amino acid-dependent ATP-diphosphate exchange assay
-
-
-
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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
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
Q5IW58, Q5IW60
-
-
-
ir
(L-alanyl)adenylate + holo-[L-alanyl-carrier protein]
AMP + L-alanyl-[L-alanyl-carrier protein]
Q5IW58, Q5IW60
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
Q5IW58, Q5IW60
-
-
-
ir
ATP + L-glutamate
diphosphate + (L-alanyl)adenylate
Q5IW58, Q5IW60
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
Q5IW58, Q5IW60
-
-
-
ir
ATP + L-glutamate + holo-[L-alanyl-carrier protein]
AMP + diphosphate + L-alanyl-[L-alanyl-carrier protein]
Q5IW58, Q5IW60
-
-
-
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4'-phosphopantetheine
phosphopantetheinylation of recombinant apoenzyme AmbE by a purified promiscuous phosphopantetheinyl transferase Sfp at pH 7.5, 28°C
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Identification of macrophage induced genes of Corynebacterium pseudotuberculosis by differential fluorescence induction.
Infections
Use of in vivo induced technology to identify antigens expressed by Photobacterium damselae subsp. piscicida during infection of Senegalese sole (Solea senegalensis).
Melanoma
Crowdsourcing natural products discovery to access uncharted dimensions of fungal metabolite diversity.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
proposed biosynthetic pathway for saframycin A involving genes sfmA, sfmB, and sfmC, overview
metabolism
Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB)is a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Production of AMB requires a five-gene cluster encoding a putative LysE-type transporter (AmbA), two non-ribosomal peptide synthetases (AmbB and AmbE, EC 6.2.1.67 and EC 6.2.1.68, respectively), and two iron(II)/alpha-ketoglutarate-dependent oxygenases (AmbC and AmbD). Bioinformatics analysis predicts one thiolation (T) domain for AmbB and two T domains (T1 and T2) for AmbE, suggesting that AMB is generated by a processing step from a precursor tripeptide assembled on a thiotemplate. The AmbB substrate is identified to be L-alanine (L-Ala), while the T1 and T2 domains of AmbE are loaded with L-glutamate (L-Glu) and L-Ala, respectively. Loading of L-Ala at T2 of AmbE occurs only in the presence of AmbB, indicative of a trans loading mechanism. In vitro assays performed with AmbB and AmbE result in the dipeptide L-Glu-L-Ala at T1 and the tripeptide L-Ala-L-Glu-L-Ala attached at T2. When AmbC and AmbD are included in the assay, these peptides are no longer detected. Instead, an L-Ala-AMB-L-Ala tripeptide is found at T2, importance of flanking L-Ala residues in the precursor tripeptide
metabolism
Q5IW58, Q5IW60
the tripeptide backbone of phosphinothricin (PT) tripeptide (PTT), a compound with herbicidal activity from Streptomyces viridochromogenes, is assembled by three stand-alone peptide synthetase modules. The enzyme PhsA (66 kDa) recruits the PT-precursor N-acetyl-demethylphosphinothricin (N-Ac-DMPT), whereas the two alanine residues of PTT are assembled by the enzymes PhsB and PhsC (129 and 119 kDa, respectively). During or after assembly, the N-Ac-DMPT residue in the peptide is converted to PT by methylation and deacetylation. Both phsB and phsC appear to be cotranscribed together with two other genes from a single promoter and they are located at a distance of 20 kb from the gene phsA, encoding PhsA, in the PTT biosynthesis gene cluster of Streptomyces viridochromogenes
metabolism
-
Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB)is a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Production of AMB requires a five-gene cluster encoding a putative LysE-type transporter (AmbA), two non-ribosomal peptide synthetases (AmbB and AmbE, EC 6.2.1.67 and EC 6.2.1.68, respectively), and two iron(II)/alpha-ketoglutarate-dependent oxygenases (AmbC and AmbD). Bioinformatics analysis predicts one thiolation (T) domain for AmbB and two T domains (T1 and T2) for AmbE, suggesting that AMB is generated by a processing step from a precursor tripeptide assembled on a thiotemplate. The AmbB substrate is identified to be L-alanine (L-Ala), while the T1 and T2 domains of AmbE are loaded with L-glutamate (L-Glu) and L-Ala, respectively. Loading of L-Ala at T2 of AmbE occurs only in the presence of AmbB, indicative of a trans loading mechanism. In vitro assays performed with AmbB and AmbE result in the dipeptide L-Glu-L-Ala at T1 and the tripeptide L-Ala-L-Glu-L-Ala attached at T2. When AmbC and AmbD are included in the assay, these peptides are no longer detected. Instead, an L-Ala-AMB-L-Ala tripeptide is found at T2, importance of flanking L-Ala residues in the precursor tripeptide
-
metabolism
-
Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB)is a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Production of AMB requires a five-gene cluster encoding a putative LysE-type transporter (AmbA), two non-ribosomal peptide synthetases (AmbB and AmbE, EC 6.2.1.67 and EC 6.2.1.68, respectively), and two iron(II)/alpha-ketoglutarate-dependent oxygenases (AmbC and AmbD). Bioinformatics analysis predicts one thiolation (T) domain for AmbB and two T domains (T1 and T2) for AmbE, suggesting that AMB is generated by a processing step from a precursor tripeptide assembled on a thiotemplate. The AmbB substrate is identified to be L-alanine (L-Ala), while the T1 and T2 domains of AmbE are loaded with L-glutamate (L-Glu) and L-Ala, respectively. Loading of L-Ala at T2 of AmbE occurs only in the presence of AmbB, indicative of a trans loading mechanism. In vitro assays performed with AmbB and AmbE result in the dipeptide L-Glu-L-Ala at T1 and the tripeptide L-Ala-L-Glu-L-Ala attached at T2. When AmbC and AmbD are included in the assay, these peptides are no longer detected. Instead, an L-Ala-AMB-L-Ala tripeptide is found at T2, importance of flanking L-Ala residues in the precursor tripeptide
-
metabolism
-
the tripeptide backbone of phosphinothricin (PT) tripeptide (PTT), a compound with herbicidal activity from Streptomyces viridochromogenes, is assembled by three stand-alone peptide synthetase modules. The enzyme PhsA (66 kDa) recruits the PT-precursor N-acetyl-demethylphosphinothricin (N-Ac-DMPT), whereas the two alanine residues of PTT are assembled by the enzymes PhsB and PhsC (129 and 119 kDa, respectively). During or after assembly, the N-Ac-DMPT residue in the peptide is converted to PT by methylation and deacetylation. Both phsB and phsC appear to be cotranscribed together with two other genes from a single promoter and they are located at a distance of 20 kb from the gene phsA, encoding PhsA, in the PTT biosynthesis gene cluster of Streptomyces viridochromogenes
-
metabolism
-
Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB)is a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Production of AMB requires a five-gene cluster encoding a putative LysE-type transporter (AmbA), two non-ribosomal peptide synthetases (AmbB and AmbE, EC 6.2.1.67 and EC 6.2.1.68, respectively), and two iron(II)/alpha-ketoglutarate-dependent oxygenases (AmbC and AmbD). Bioinformatics analysis predicts one thiolation (T) domain for AmbB and two T domains (T1 and T2) for AmbE, suggesting that AMB is generated by a processing step from a precursor tripeptide assembled on a thiotemplate. The AmbB substrate is identified to be L-alanine (L-Ala), while the T1 and T2 domains of AmbE are loaded with L-glutamate (L-Glu) and L-Ala, respectively. Loading of L-Ala at T2 of AmbE occurs only in the presence of AmbB, indicative of a trans loading mechanism. In vitro assays performed with AmbB and AmbE result in the dipeptide L-Glu-L-Ala at T1 and the tripeptide L-Ala-L-Glu-L-Ala attached at T2. When AmbC and AmbD are included in the assay, these peptides are no longer detected. Instead, an L-Ala-AMB-L-Ala tripeptide is found at T2, importance of flanking L-Ala residues in the precursor tripeptide
-
metabolism
-
Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB)is a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Production of AMB requires a five-gene cluster encoding a putative LysE-type transporter (AmbA), two non-ribosomal peptide synthetases (AmbB and AmbE, EC 6.2.1.67 and EC 6.2.1.68, respectively), and two iron(II)/alpha-ketoglutarate-dependent oxygenases (AmbC and AmbD). Bioinformatics analysis predicts one thiolation (T) domain for AmbB and two T domains (T1 and T2) for AmbE, suggesting that AMB is generated by a processing step from a precursor tripeptide assembled on a thiotemplate. The AmbB substrate is identified to be L-alanine (L-Ala), while the T1 and T2 domains of AmbE are loaded with L-glutamate (L-Glu) and L-Ala, respectively. Loading of L-Ala at T2 of AmbE occurs only in the presence of AmbB, indicative of a trans loading mechanism. In vitro assays performed with AmbB and AmbE result in the dipeptide L-Glu-L-Ala at T1 and the tripeptide L-Ala-L-Glu-L-Ala attached at T2. When AmbC and AmbD are included in the assay, these peptides are no longer detected. Instead, an L-Ala-AMB-L-Ala tripeptide is found at T2, importance of flanking L-Ala residues in the precursor tripeptide
-
metabolism
-
Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB)is a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Production of AMB requires a five-gene cluster encoding a putative LysE-type transporter (AmbA), two non-ribosomal peptide synthetases (AmbB and AmbE, EC 6.2.1.67 and EC 6.2.1.68, respectively), and two iron(II)/alpha-ketoglutarate-dependent oxygenases (AmbC and AmbD). Bioinformatics analysis predicts one thiolation (T) domain for AmbB and two T domains (T1 and T2) for AmbE, suggesting that AMB is generated by a processing step from a precursor tripeptide assembled on a thiotemplate. The AmbB substrate is identified to be L-alanine (L-Ala), while the T1 and T2 domains of AmbE are loaded with L-glutamate (L-Glu) and L-Ala, respectively. Loading of L-Ala at T2 of AmbE occurs only in the presence of AmbB, indicative of a trans loading mechanism. In vitro assays performed with AmbB and AmbE result in the dipeptide L-Glu-L-Ala at T1 and the tripeptide L-Ala-L-Glu-L-Ala attached at T2. When AmbC and AmbD are included in the assay, these peptides are no longer detected. Instead, an L-Ala-AMB-L-Ala tripeptide is found at T2, importance of flanking L-Ala residues in the precursor tripeptide
-
metabolism
-
Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB)is a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Production of AMB requires a five-gene cluster encoding a putative LysE-type transporter (AmbA), two non-ribosomal peptide synthetases (AmbB and AmbE, EC 6.2.1.67 and EC 6.2.1.68, respectively), and two iron(II)/alpha-ketoglutarate-dependent oxygenases (AmbC and AmbD). Bioinformatics analysis predicts one thiolation (T) domain for AmbB and two T domains (T1 and T2) for AmbE, suggesting that AMB is generated by a processing step from a precursor tripeptide assembled on a thiotemplate. The AmbB substrate is identified to be L-alanine (L-Ala), while the T1 and T2 domains of AmbE are loaded with L-glutamate (L-Glu) and L-Ala, respectively. Loading of L-Ala at T2 of AmbE occurs only in the presence of AmbB, indicative of a trans loading mechanism. In vitro assays performed with AmbB and AmbE result in the dipeptide L-Glu-L-Ala at T1 and the tripeptide L-Ala-L-Glu-L-Ala attached at T2. When AmbC and AmbD are included in the assay, these peptides are no longer detected. Instead, an L-Ala-AMB-L-Ala tripeptide is found at T2, importance of flanking L-Ala residues in the precursor tripeptide
-
metabolism
-
proposed biosynthetic pathway for saframycin A involving genes sfmA, sfmB, and sfmC, overview
-
metabolism
-
Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB)is a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Production of AMB requires a five-gene cluster encoding a putative LysE-type transporter (AmbA), two non-ribosomal peptide synthetases (AmbB and AmbE, EC 6.2.1.67 and EC 6.2.1.68, respectively), and two iron(II)/alpha-ketoglutarate-dependent oxygenases (AmbC and AmbD). Bioinformatics analysis predicts one thiolation (T) domain for AmbB and two T domains (T1 and T2) for AmbE, suggesting that AMB is generated by a processing step from a precursor tripeptide assembled on a thiotemplate. The AmbB substrate is identified to be L-alanine (L-Ala), while the T1 and T2 domains of AmbE are loaded with L-glutamate (L-Glu) and L-Ala, respectively. Loading of L-Ala at T2 of AmbE occurs only in the presence of AmbB, indicative of a trans loading mechanism. In vitro assays performed with AmbB and AmbE result in the dipeptide L-Glu-L-Ala at T1 and the tripeptide L-Ala-L-Glu-L-Ala attached at T2. When AmbC and AmbD are included in the assay, these peptides are no longer detected. Instead, an L-Ala-AMB-L-Ala tripeptide is found at T2, importance of flanking L-Ala residues in the precursor tripeptide
-
physiological function
the enzyme is involved in biosynthesis of Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB), which proceeds via a precursor tripeptide. Identification of the building blocks of AMB biosynthesis and modelling, overview
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 nonribosomal peptide synthetase (NRPS) system
physiological function
Q5IW58, Q5IW60
the tripeptide backbone of phosphinothricin (PT) tripeptide (PTT), a compound with herbicidal activity from Streptomyces viridochromogenes, is assembled by three stand-alone peptide synthetase modules. The enzyme PhsA (66 kDa) recruits the PT-precursor N-acetyl-demethylphosphinothricin (N-Ac-DMPT), whereas the two alanine residues of PTT are assembled by the enzymes PhsB and PhsC (129 and 119 kDa, respectively). During or after assembly, the N-Ac-DMPT residue in the peptide is converted to PT by methylation and deacetylation. PhsB and PhsC represent single nonribosomal peptide synthetase elongation modules lacking a thioesterase domain
physiological function
Q5IW58, Q5IW60
the tripeptide backbone of phosphinothricin (PT) tripeptide (PTT), a compound with herbicidal activity from Streptomyces viridochromogenes, is assembled by three stand-alone peptide synthetase modules. The enzyme PhsA (66 kDa) recruits the PT-precursor N-acetyl-demethylphosphinothricin (N-Ac-DMPT), whereas the two alanine residues of PTT are assembled by the enzymes PhsB and PhsC (129 and 119 kDa, respectively). During or after assembly, the N-Ac-DMPT residue in the peptide is converted to PT by methylation and deacetylation. PhsB and PhsC represent single nonribosomal peptide synthetase elongation modules lacking a thioesterase domain. Gene inactivations, genetic complementations, determinations of substrate specificity of the heterologously produced proteins, and comparison of PhsC sequence with the N-terminus of the alanine-activating nonribosomal peptide synthetase PTTSII from Streptomyces viridochromogenes confirm the role of the two genes in the bialanylation of Ac-DMPT. The lack of an integral thioesterase domain in the PTT assembly system points to product release possibly involving two type II thioesterase genes (the1 and the2) located in the PTT gene cluster alone or in conjunction with another mechanism of product release
physiological function
-
the enzyme is involved in biosynthesis of Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB), which proceeds via a precursor tripeptide. Identification of the building blocks of AMB biosynthesis and modelling, overview
-
physiological function
-
the enzyme is involved in biosynthesis of Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB), which proceeds via a precursor tripeptide. Identification of the building blocks of AMB biosynthesis and modelling, overview
-
physiological function
-
the tripeptide backbone of phosphinothricin (PT) tripeptide (PTT), a compound with herbicidal activity from Streptomyces viridochromogenes, is assembled by three stand-alone peptide synthetase modules. The enzyme PhsA (66 kDa) recruits the PT-precursor N-acetyl-demethylphosphinothricin (N-Ac-DMPT), whereas the two alanine residues of PTT are assembled by the enzymes PhsB and PhsC (129 and 119 kDa, respectively). During or after assembly, the N-Ac-DMPT residue in the peptide is converted to PT by methylation and deacetylation. PhsB and PhsC represent single nonribosomal peptide synthetase elongation modules lacking a thioesterase domain
-
physiological function
-
the tripeptide backbone of phosphinothricin (PT) tripeptide (PTT), a compound with herbicidal activity from Streptomyces viridochromogenes, is assembled by three stand-alone peptide synthetase modules. The enzyme PhsA (66 kDa) recruits the PT-precursor N-acetyl-demethylphosphinothricin (N-Ac-DMPT), whereas the two alanine residues of PTT are assembled by the enzymes PhsB and PhsC (129 and 119 kDa, respectively). During or after assembly, the N-Ac-DMPT residue in the peptide is converted to PT by methylation and deacetylation. PhsB and PhsC represent single nonribosomal peptide synthetase elongation modules lacking a thioesterase domain. Gene inactivations, genetic complementations, determinations of substrate specificity of the heterologously produced proteins, and comparison of PhsC sequence with the N-terminus of the alanine-activating nonribosomal peptide synthetase PTTSII from Streptomyces viridochromogenes confirm the role of the two genes in the bialanylation of Ac-DMPT. The lack of an integral thioesterase domain in the PTT assembly system points to product release possibly involving two type II thioesterase genes (the1 and the2) located in the PTT gene cluster alone or in conjunction with another mechanism of product release
-
physiological function
-
the enzyme is involved in biosynthesis of Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB), which proceeds via a precursor tripeptide. Identification of the building blocks of AMB biosynthesis and modelling, overview
-
physiological function
-
the enzyme is involved in biosynthesis of Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB), which proceeds via a precursor tripeptide. Identification of the building blocks of AMB biosynthesis and modelling, overview
-
physiological function
-
the enzyme is involved in biosynthesis of Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB), which proceeds via a precursor tripeptide. Identification of the building blocks of AMB biosynthesis and modelling, overview
-
physiological function
-
the enzyme is involved in biosynthesis of Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB), which proceeds via a precursor tripeptide. Identification of the building blocks of AMB biosynthesis and modelling, overview
-
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 nonribosomal peptide synthetase (NRPS) system
-
physiological function
-
the enzyme is involved in biosynthesis of Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoicacid (AMB), which proceeds via a precursor tripeptide. Identification of the building blocks of AMB biosynthesis and modelling, overview
-
additional information
enzyme AmbB presents the typical modular structure of non-ribosomal peptide synthetases (NRPSs)
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
-
enzyme AmbB presents the typical modular structure of non-ribosomal peptide synthetases (NRPSs)
-
additional information
-
enzyme AmbB presents the typical modular structure of non-ribosomal peptide synthetases (NRPSs)
-
additional information
-
enzyme AmbB presents the typical modular structure of non-ribosomal peptide synthetases (NRPSs)
-
additional information
-
enzyme AmbB presents the typical modular structure of non-ribosomal peptide synthetases (NRPSs)
-
additional information
-
enzyme AmbB presents the typical modular structure of non-ribosomal peptide synthetases (NRPSs)
-
additional information
-
enzyme AmbB presents the typical modular structure of non-ribosomal peptide synthetases (NRPSs)
-
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
-
enzyme AmbB presents the typical modular structure of non-ribosomal peptide synthetases (NRPSs)
-
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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). AMBB_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
1249
0
134447
Swiss-Prot
-
PHSB_STRVT
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
1189
0
129117
Swiss-Prot
-
PHSC_STRVT
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
1086
0
118822
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
modular structure of AmbE with domains for adenylation, thiolation, condensation, methylation, and thioester cleavage. AmbE may have an additional domain of unknown function at its N-terminus and the C domain is atypical, domain architecture, overview
additional information
-
modular structure of AmbE with domains for adenylation, thiolation, condensation, methylation, and thioester cleavage. AmbE may have an additional domain of unknown function at its N-terminus and the C domain is atypical, domain architecture, overview
-
additional information
-
modular structure of AmbE with domains for adenylation, thiolation, condensation, methylation, and thioester cleavage. AmbE may have an additional domain of unknown function at its N-terminus and the C domain is atypical, domain architecture, overview
-
additional information
-
modular structure of AmbE with domains for adenylation, thiolation, condensation, methylation, and thioester cleavage. AmbE may have an additional domain of unknown function at its N-terminus and the C domain is atypical, domain architecture, overview
-
additional information
-
modular structure of AmbE with domains for adenylation, thiolation, condensation, methylation, and thioester cleavage. AmbE may have an additional domain of unknown function at its N-terminus and the C domain is atypical, domain architecture, overview
-
additional information
-
modular structure of AmbE with domains for adenylation, thiolation, condensation, methylation, and thioester cleavage. AmbE may have an additional domain of unknown function at its N-terminus and the C domain is atypical, domain architecture, overview
-
additional information
-
modular structure of AmbE with domains for adenylation, thiolation, condensation, methylation, and thioester cleavage. AmbE may have an additional domain of unknown function at its N-terminus and the C domain is atypical, domain architecture, overview
-
additional information
-
modular structure of AmbE with domains for adenylation, thiolation, condensation, methylation, and thioester cleavage. AmbE may have an additional domain of unknown function at its N-terminus and the C domain is atypical, domain architecture, overview
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Q5IW58
gene disruption mutagenesis in phsC using the temperature-sensitive plasmid pDS104 is performed. Mutants PHSB and PHSBC are generated using the nonreplicative plasmids pMS100 and pDS199, respectively, complementation of the mutants PHSB and PHSBC and heterologous expression of phsB/phsC in Streptomyces lividans. Construction of a phsB null mutant (B3-14), which is unable to produce phosphinothricin tripeptide (PTT), no alanine-activating activity attributable to PTT synthetase III is detected. Construction of a triple PTT mutant (phsB, orfM, and phsC), mutant PHSBC has lost the ability to produce PTT. Transformation of PHSBC with either phsB including orfM (pDS207) or phsC (pDS208) does not restore PTT synthesis, indicating that PhsB cannot take on the function of PhsC or vice versa
additional information
Q5IW60
gene disruption mutagenesis in phsC using the temperature-sensitive plasmid pDS104 is performed. Mutants PHSB and PHSBC are generated using the nonreplicative plasmids pMS100 and pDS199, respectively, complementation of the mutants PHSB and PHSBC and heterologous expression of phsB/phsC in Streptomyces lividans. Construction of a phsB null mutant (B3-14), which is unable to produce phosphinothricin tripeptide (PTT), no alanine-activating activity attributable to PTT synthetase III is detected. Construction of a triple PTT mutant (phsB, orfM, and phsC), mutant PHSBC has lost the ability to produce PTT. Transformation of PHSBC with either phsB including orfM (pDS207) or phsC (pDS208) does not restore PTT synthesis, indicating that PhsB cannot take on the function of PhsC or vice versa
additional information
Q5IW58
gene disruption mutagenesis in phsC using the temperature-sensitive plasmid pDS104 is performed. Mutants PHSB and PHSBC are generated using the nonreplicative plasmids pMS100 and pDS199, respectively, complementation of the mutants PHSB and PHSBC and heterologous expression of phsB/phsC in Streptomyces lividans. No activity attributable to PTT synthetase II or phosphinothricin tripeptide (PTT) synthesis is detected in the phsC disruption mutant. Construction of a triple PTT mutant (phsB, orfM, and phsC), mutant PHSBC has lost the ability to produce PTT. Transformation of PHSBC with either phsB including orfM (pDS207) or phsC (pDS208) does not restore PTT synthesis, indicating that PhsB cannot take on the function of PhsC or vice versa
additional information
Q5IW60
gene disruption mutagenesis in phsC using the temperature-sensitive plasmid pDS104 is performed. Mutants PHSB and PHSBC are generated using the nonreplicative plasmids pMS100 and pDS199, respectively, complementation of the mutants PHSB and PHSBC and heterologous expression of phsB/phsC in Streptomyces lividans. No activity attributable to PTT synthetase II or phosphinothricin tripeptide (PTT) synthesis is detected in the phsC disruption mutant. Construction of a triple PTT mutant (phsB, orfM, and phsC), mutant PHSBC has lost the ability to produce PTT. Transformation of PHSBC with either phsB including orfM (pDS207) or phsC (pDS208) does not restore PTT synthesis, indicating that PhsB cannot take on the function of PhsC or vice versa
additional information
-
gene disruption mutagenesis in phsC using the temperature-sensitive plasmid pDS104 is performed. Mutants PHSB and PHSBC are generated using the nonreplicative plasmids pMS100 and pDS199, respectively, complementation of the mutants PHSB and PHSBC and heterologous expression of phsB/phsC in Streptomyces lividans. No activity attributable to PTT synthetase II or phosphinothricin tripeptide (PTT) synthesis is detected in the phsC disruption mutant. Construction of a triple PTT mutant (phsB, orfM, and phsC), mutant PHSBC has lost the ability to produce PTT. Transformation of PHSBC with either phsB including orfM (pDS207) or phsC (pDS208) does not restore PTT synthesis, indicating that PhsB cannot take on the function of PhsC or vice versa
-
additional information
-
gene disruption mutagenesis in phsC using the temperature-sensitive plasmid pDS104 is performed. Mutants PHSB and PHSBC are generated using the nonreplicative plasmids pMS100 and pDS199, respectively, complementation of the mutants PHSB and PHSBC and heterologous expression of phsB/phsC in Streptomyces lividans. Construction of a phsB null mutant (B3-14), which is unable to produce phosphinothricin tripeptide (PTT), no alanine-activating activity attributable to PTT synthetase III is detected. Construction of a triple PTT mutant (phsB, orfM, and phsC), mutant PHSBC has lost the ability to produce PTT. Transformation of PHSBC with either phsB including orfM (pDS207) or phsC (pDS208) does not restore PTT synthesis, indicating that PhsB cannot take on the function of PhsC or vice versa
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from mycelium by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography
Q5IW58, Q5IW60
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)/pLys by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ambB, encoded in the amb gene cluster, genetic organization, recombinant overexpression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)/pLys
gene phsB, DNA and amino acid sequence determination and analysis, promoter analysis, both phsB and phsC appear to be cotranscribed together with two other genes from a single promoter, and they are located at a distance of 20 kb from the gene phsA, encoding PhsA, in the PTT biosynthesis gene cluster, heterologous coexpression of phsB/phsC in Streptomyces lividans strain TK23 using vector pDS209
Q5IW58, Q5IW60
gene phsC, DNA and amino acid sequence determination and analysis, promoter analysis, both phsB and phsC appear to be cotranscribed together with two other genes from a single promoter, and they are located at a distance of 20 kb from the gene phsA, encoding PhsA, in the PTT biosynthesis gene cluster, heterologous coexpression of phsB/phsC in Streptomyces lividans strain TK23 using vector pDS209
Q5IW58, Q5IW60
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 sfmA, part of the SFM-A gene cluster, DNA and amino acid sequence determination and analysis, genetic organization, recombinant expression in Pseudomonas fluorescens
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schwartz, D.; Grammel, N.; Heinzelmann, E.; Keller, U.; Wohlleben, W.
Phosphinothricin tripeptide synthetases in Streptomyces viridochromogenes T494
Antimicrob. Agents Chemother.
49
4598-4607
2005
Streptomyces viridochromogenes (Q5IW58), Streptomyces viridochromogenes (Q5IW60), Streptomyces viridochromogenes T494 (Q5IW58), Streptomyces viridochromogenes T494 (Q5IW60)
brenda
Murcia, N.; Lee, X.; Waridel, P.; Maspoli, A.; Imker, H.; Chai, T.; Walsh, C.; Reimmann, C.
The Pseudomonas aeruginosa antimetabolite L-2-amino-4-methoxy-trans-3-butenoic acid (AMB) is made from glutamate and two alanine residues via a thiotemplate-linked tripeptide precursor
Front. Microbiol.
6
170
2015
Pseudomonas aeruginosa (Q9I1H0), Pseudomonas aeruginosa ATCC 15692 (Q9I1H0), Pseudomonas aeruginosa 1C (Q9I1H0), Pseudomonas aeruginosa PRS 101 (Q9I1H0), Pseudomonas aeruginosa DSM 22644 (Q9I1H0), Pseudomonas aeruginosa CIP 104116 (Q9I1H0), Pseudomonas aeruginosa LMG 12228 (Q9I1H0), Pseudomonas aeruginosa JCM 14847 (Q9I1H0)
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 (B0CN25), Streptomyces lavendulae NRRL 11002 (B0CN25)
brenda
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