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Information on EC 1.3.3.16 - oxazoline dehydrogenase

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EC Tree
     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.16 oxazoline dehydrogenase
IUBMB Comments
Contains FMN. This enzyme oxidizes 2-oxazoline, 5-methyl-2-oxazoline, and 2-thiazoline within peptides, which were formed by EC 6.2.2.2, oxazoline synthase, and EC 6.2.2.3, thiazoline synthase, to the respective pyrrole-type rings. The enzyme is found as either a stand-alone protein or as a domain within a multifunctional protein (the G protein) that also functions as a peptidase.
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This record set is specific for:
UNIPROT: P23186 not found.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
thcox, microcin b17 synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
artG
-
-
-
-
azoline oxidase
-
-
-
-
cyanobactin oxidase
-
-
-
-
lynG
-
-
-
-
mcaG
-
-
-
-
McbB
P23184; P23185; P23186
-
McbC
P23184; P23185; P23186
-
McbD
P23184; P23185; P23186
-
microcin B17 synthase
P23184; P23185; P23186
-
microcin B17-processing protein McbC
-
tenG
-
-
-
-
thiazoline oxidase
-
-
-
-
thiazoline oxidase/subtilisin-like protease
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline + O2 = a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole + H2O2
show the reaction diagram
(1)
-
-
-
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline + O2 = a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole + H2O2
show the reaction diagram
(2)
-
-
-
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline + O2 = a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-1,3-oxazole + H2O2
show the reaction diagram
(3)
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
a [protein]-2-oxazoline:oxygen oxidoreductase (2-oxazole-forming)
Contains FMN. This enzyme oxidizes 2-oxazoline, 5-methyl-2-oxazoline, and 2-thiazoline within peptides, which were formed by EC 6.2.2.2, oxazoline synthase, and EC 6.2.2.3, thiazoline synthase, to the respective pyrrole-type rings. The enzyme is found as either a stand-alone protein or as a domain within a multifunctional protein (the G protein) that also functions as a peptidase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline + O2
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole + H2O2
show the reaction diagram
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline + O2
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole + H2O2
show the reaction diagram
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline + O2
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-1,3-oxazole + H2O2
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline + O2
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole + H2O2
show the reaction diagram
P23184; P23185; P23186
-
-
-
?
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline + O2
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole + H2O2
show the reaction diagram
P23184; P23185; P23186
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
each McbC subunit contributes to the binding of the FMN cofactor molecules, with Arg82 of one McbC subunit and Arg117 of the other forming salt bridges with the phosphate group and Arg181 interacting with the O2 of FMN
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B8HTZ1_CYAP4
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
473
0
52963
TrEMBL
-
MCBC_ECOLX
272
0
30753
Swiss-Prot
other Location (Reliability: 2)
Q52QJ1_PRODI
1191
0
130557
TrEMBL
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
P23184; P23185; P23186
x * 33000, subunit McbB, x * 31000, subunit McbC, x * 45000, subunit McbD, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 3.15 A resolution, space group P412121 with two molecules found in the asymmetric unit. The structure is composed of a novel domain and an FMN nitroreductase domain. The N-terminal domain contains a portion (residues 7-86) which possesses the same fold as the leader binding domain of TruD, the so-called peptide-clamp domain. The C-terminal domain (residues 323-469) contains the FMN molecule and has a high degree of homology to the putative nitroreductase from Anabaena variabilis
structures of synthetase McbBCD reveal an octameric B4C2D2 complex with two bound substrate peptides. Each McbB dimer clamps the N-terminal recognition sequence, while the C-terminal heterocycle of the modified peptide is trapped in the active site of McbC. The McbD and McbC active sites are distant from each other, which necessitates alternate shuttling of the peptide substrate between them, while remaining tethered to the McbB dimer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of the modified McbA peptide together with all three components of the microcin B17 synthetase as a stable complex
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bent, A.F.; Mann, G.; Houssen, W.E.; Mykhaylyk, V.; Duman, R.; Thomas, L.; Jaspars, M.; Wagner, A.; Naismith, J.H.
Structure of the cyanobactin oxidase ThcOx fromCyanothece sp. PCC 7425, the first structure to be solved at Diamond Light Source beamline I23 by means of S-SAD
Acta Crystallogr. Sect. D
72
1174-1180
2016
Cyanothece sp. PCC 7425 (B8HTZ1)
Manually annotated by BRENDA team
Ghilarov, D.; Stevenson, C.EM.; Travin, D.Y.; Piskunova, J.; Serebryakova, M.; Maxwell, A.; Lawson, D.M.; Severinov, K.
Architecture of microcin B17 synthetase an octameric protein complex converting a ribosomally synthesized peptide into a DNA gyrase poison
Mol. Cell
73
749-762
2019
Escherichia coli (P23185)
Manually annotated by BRENDA team
Schmidt, E.W.; Nelson, J.T.; Rasko, D.A.; Sudek, S.; Eisen, J.A.; Haygood, M.G.; Ravel, J.
Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella
Proc. Natl. Acad. Sci. USA
102
7315-7320
2005
Prochloron didemni (Q52QJ1)
Manually annotated by BRENDA team
Li, Y.M.; Milne, J.C.; Madison, L.L.; Kolter, R.; Walsh, C.T.
From peptide precursors to oxazole and thiazole-containing peptide antibiotics microcin B17 synthase
Science
274
1188-1193
1996
Escherichia coli (P23184 and P23185 and P23186)
Manually annotated by BRENDA team