KEGG   ENZYME: 1.3.3.16
Entry
EC 1.3.3.16                 Enzyme                                 

Name
oxazoline dehydrogenase;
azoline oxidase;
thiazoline oxidase;
cyanobactin oxidase;
patG (gene name);
mcaG (gene name);
artG (gene name);
lynG (gene name);
tenG (gene name)
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With oxygen as acceptor
Sysname
a [protein]-2-oxazoline:oxygen oxidoreductase (2-oxazole-forming)
Reaction(IUBMB)
(1) 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;
(2) 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;
(3) 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
Substrate
[protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline;
O2 [CPD:C00007];
[protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline;
[protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline
Product
[protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole;
H2O2 [CPD:C00027];
[protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole;
[protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-1,3-oxazole
Comment
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.
History
EC 1.3.3.16 created 2020
Orthology
K05897  oxazoline/thiazoline dehydrogenase
K24454  thiazoline dehydrogenase / protease
Genes
SVR: CP971_15255
ATL: Athai_48170
LEP: Lepto7376_0890
CYJ: Cyan7822_6148 Cyan7822_6534
CYN: Cyan7425_0520
TER: Tery_2359
MIC: Mic7113_0885
ARP: NIES39_O00960
ONI: Osc7112_3655
MPRO: BJP34_18465
FTJ: FTUN_1197
 » show all
Reference
1  [PMID:8895467]
  Authors
Li YM, Milne JC, Madison LL, Kolter R, Walsh CT
  Title
From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase.
  Journal
Science 274:1188-93 (1996)
DOI:10.1126/science.274.5290.1188
Reference
2  [PMID:15883371]
  Authors
Schmidt EW, Nelson JT, Rasko DA, Sudek S, Eisen JA, Haygood MG, Ravel J
  Title
Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella.
  Journal
Proc Natl Acad Sci U S A 102:7315-20 (2005)
DOI:10.1073/pnas.0501424102
  Sequence
Reference
3  [PMID:27841750]
  Authors
Bent AF, Mann G, Houssen WE, Mykhaylyk V, Duman R, Thomas L, Jaspars M, Wagner A, Naismith JH
  Title
Structure of the cyanobactin oxidase ThcOx from Cyanothece sp. PCC 7425, the first structure to be solved at Diamond Light Source beamline I23 by means of S-SAD.
  Journal
Acta Crystallogr D Struct Biol 72:1174-1180 (2016)
DOI:10.1107/S2059798316015850
  Sequence
Reference
4  [PMID:30661981]
  Authors
Ghilarov D, Stevenson CEM, Travin DY, Piskunova J, Serebryakova M, Maxwell A, Lawson DM, Severinov K
  Title
Architecture of Microcin B17 Synthetase: An Octameric Protein Complex Converting  a Ribosomally Synthesized Peptide into a DNA Gyrase Poison.
  Journal
Mol Cell 73:749-762.e5 (2019)
DOI:10.1016/j.molcel.2018.11.032
Other DBs
ExplorEnz - The Enzyme Database: 1.3.3.16
IUBMB Enzyme Nomenclature: 1.3.3.16
ExPASy - ENZYME nomenclature database: 1.3.3.16
BRENDA, the Enzyme Database: 1.3.3.16

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