KEGG   ENZYME: 1.13.11.18Help
Entry
EC 1.13.11.18               Enzyme                                 

Name
sulfur dioxygenase;
sulfur oxygenase;
sulfur:oxygen oxidoreductase
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
BRITE hierarchy
Sysname
S-sulfanylglutathione:oxygen oxidoreductase
Reaction(IUBMB)
sulfur + O2 + H2O = sulfite + 2 H+ (overall reaction) [RN:R00781];
(1a) glutathione + sulfur = S-sulfanylglutathione (spontaneous) [RN:R08677];
(1b) S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+ [RN:R08678]
Reaction(KEGG)
Substrate
sulfur [CPD:C00087];
O2 [CPD:C00007];
H2O [CPD:C00001];
glutathione [CPD:C00051];
S-sulfanylglutathione [CPD:C17267]
Product
sulfite [CPD:C00094];
H+ [CPD:C00080];
S-sulfanylglutathione [CPD:C17267];
glutathione [CPD:C00051]
Comment
An iron protein. Glutathione (GSH) plays a catalytic role in elemental sulfur activation, but is not consumed during the enzymic reaction. GSH and elemental sulfur react non-enzymically to yield S-sulfanylglutathione and it is only in this form that the sulfur can be oxidized to yield sulfite. The sulfite can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].
History
EC 1.13.11.18 created 1972
Pathway
Sulfur metabolism
Microbial metabolism in diverse environments
Orthology
K17725  
sulfur dioxygenase
Genes
HSA: 
23474(ETHE1)
PTR: 
456093(ETHE1)
PPS: 
100983420(ETHE1)
GGO: 
101138346(ETHE1)
PON: 
100458034(ETHE1)
MCC: 
718089(ETHE1)
MCF: 
102135821(ETHE1)
MMU: 
66071(Ethe1)
RNO: 
292710(Ethe1)
CGE: 
100769786(Ethe1)
HGL: 
101700567(Ethe1)
TUP: 
102495095(ETHE1)
CFA: 
612416(ETHE1)
AML: 
FCA: 
101092565(ETHE1)
PTG: 
102966568(ETHE1)
BTA: 
509150(ETHE1)
BOM: 
102274866(ETHE1)
PHD: 
102330175(ETHE1)
CHX: 
102183356(ETHE1)
SSC: 
100523003(ETHE1)
CFR: 
102515553(ETHE1)
BACU: 
103015695(ETHE1)
LVE: 
103088914(ETHE1)
ECB: 
100146195(ETHE1)
MYB: 
102243740(ETHE1)
MYD: 
102751781(ETHE1)
PALE: 
102885174(ETHE1)
GGA: 
426450(ETHE1)
PHI: 
ASN: 
102372675(ETHE1)
AMJ: 
102565248(ETHE1)
CMY: 
ACS: 
PBI: 
103054622(ETHE1)
XLA: 
379091(ethe1)
XTR: 
448221(ethe1)
DRE: 
405865(ethe1)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
BFO: 
CIN: 
SPU: 
DME: 
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DAN: 
DER: 
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DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
410023(GB14390) 551510(GB12363)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CBR: 
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
ATH: 
AT1G53580(GLY3)
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
CAM: 
FVE: 
PPER: 
CSV: 
RCU: 
POP: 
POPTR_0001s38910g(POPTRDRAFT_749057) POPTR_0005s22640g(POPTRDRAFT_831572)
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os01t0667200-01(Os01g0667200)
OBR: 
BDI: 
SBI: 
SORBI_03g030620(SORBIDRAFT_03g030620)
ZMA: 
100283164(IDP546)
SITA: 
ATR: 
s00014p00246150(AMTR_s00014p00246150)
SMO: 
PPP: 
OLU: 
OTA: 
MIS: 
MPP: 
BPG: 
GSL: 
PTI: 
TPS: 
NGD: 
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NGR: 
 » show all
Taxonomy
Reference
1  [PMID:5968172]
  Authors
Suzuki I, Silver M.
  Title
The initial product and properties of the sulfur-oxidizing enzyme of thiobacilli.
  Journal
Biochim. Biophys. Acta. 122 (1966) 22-33.
  Organism
Thiobacillus thioparus, Thiobacillus thiooxidans
Reference
2  [PMID:12855721]
  Authors
Rohwerder T, Sand W.
  Title
The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp.
  Journal
Microbiology. 149 (2003) 1699-710.
  Organism
Acidiphilium acidophilum, Acidithiobacillus ferrooxidans, Acidithiobacillus thiooxidans
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37256-58-9

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