KEGG   ENZYME: 1.13.11.18Help
Entry
EC 1.13.11.18               Enzyme                                 

Name
persulfide dioxygenase;
sulfur oxygenase (incorrect);
sulfur:oxygen oxidoreductase (incorrect);
sulfur dioxygenase (incorrect)
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)
S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+ (overall reaction) [RN:R08678];
(1a) S-sulfanylglutathione + O2 = S-sulfinatoglutathione + H+ [RN:R11946];
(1b) S-sulfinatoglutathione + H2O = glutathione + sulfite + H+ (spontaneous) [RN:R11947]
Reaction(KEGG)
Substrate
S-sulfanylglutathione [CPD:C17267];
O2 [CPD:C00007];
H2O [CPD:C00001];
S-sulfinatoglutathione [CPD:C21787]
Product
glutathione [CPD:C00051];
sulfite [CPD:C00094];
H+ [CPD:C00080];
S-sulfinatoglutathione [CPD:C21787]
Comment
An iron protein. Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme. The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].
History
EC 1.13.11.18 created 1972, modified 2015
Pathway
ec00920  Sulfur metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K17725  sulfur dioxygenase
Genes
HSA: 23474(ETHE1)
PTR: 456093(ETHE1)
PON: 100458034(ETHE1)
NLE: 100607326(ETHE1)
MCC: 718089(ETHE1)
MCF: 102135821(ETHE1)
CSAB: 103234782(ETHE1)
RRO: 104669456(ETHE1)
RBB: 108538048(ETHE1)
CJC: 100392539(ETHE1)
SBQ: 101049584(ETHE1)
MMU: 66071(Ethe1)
RNO: 292710(Ethe1)
CGE: 100769786(Ethe1)
NGI: 103749149(Ethe1)
HGL: 101700567(Ethe1)
CCAN: 109691867(Ethe1)
OCU: 100340123(ETHE1)
TUP: 102495095(ETHE1)
CFA: 612416(ETHE1)
AML: 100470121(ETHE1)
UMR: 103657004(ETHE1)
ORO: 101379540(ETHE1)
FCA: 101092565(ETHE1)
PTG: 102966568(ETHE1)
AJU: 106973678(ETHE1)
BTA: 509150(ETHE1)
BOM: 102274866(ETHE1)
BIU: 109572865(ETHE1)
PHD: 102330175(ETHE1)
CHX: 102183356(ETHE1)
OAS: 101108154(ETHE1)
SSC: 106504117(ETHE1)
CFR: 102515553(ETHE1)
CDK: 105090237(ETHE1)
BACU: 103015695(ETHE1)
LVE: 103088914(ETHE1)
OOR: 101277675(ETHE1)
ECB: 100146195(ETHE1)
EPZ: 103550890(ETHE1)
EAI: 106848399(ETHE1)
MYB: 102243740(ETHE1)
MYD: 102751781(ETHE1)
HAI: 109372823(ETHE1)
RSS: 109442569 109460827(ETHE1)
PALE: 102885174(ETHE1)
LAV: 100654574(ETHE1)
TMU: 101349750
SHR: 100919768(ETHE1)
OAA: 107546927(ETHE1)
CJO: 107307773(ETHE1)
PHI: 106628866(ETHE1)
ASN: 102372675(ETHE1)
AMJ: 102565248(ETHE1)
CMY: 102948016
CPIC: 101936154 101940172(ETHE1)
ACS: 100561649(ethe1)
PVT: 110089614(ETHE1)
PBI: 103054622
GJA: 107122195(ETHE1)
XLA: 108704965(ethe1.S) 379091(ethe1.L)
XTR: 448221(ethe1)
NPR: 108785537(ETHE1)
DRE: 405865(ethe1)
SRX: 107724764(ethe1)
SANH: 107673323(ethe1)
IPU: 108278065(ethe1)
AMEX: 111197379(ethe1)
TRU: 101079181(ethe1)
LCO: 104930280(ethe1)
NCC: 104950320(ethe1)
OLA: 101159221(ethe1)
CSEM: 103388847(ethe1)
LCF: 108899420(ethe1)
SDU: 111235762(ethe1)
HCQ: 109513105(ethe1)
BPEC: 110168222(ethe1)
SASA: 106582613(ETHE1) 106605166
ELS: 105008890(ethe1)
SFM: 108919204(ethe1)
LCM: 102365540(ETHE1)
SPU: 585574
APLC: 110988524
DME: Dmel_CG30022(CG30022) Dmel_CG30023(sprt)
DSI: Dsimw501_GD25902(Dsim_GD25902) Dsimw501_GD28368(Dsim_GD28368)
PXY: 105388838
CEL: CELE_C33A12.7(ethe-1)
CBR: CBG20009
CRG: 105329868
MYI: 110443462
OBI: 106871303
SHX: MS3_00676
EGL: EGR_05903
ADF: 107343924
HMG: 100205916
ATH: AT1G53580(GLY3)
CRB: 17897233
THJ: 104822594
CPAP: 110812511
CIT: 102607739
GMX: 100780846(GMGLYII-6) 100796796(GMGLYII-10)
VRA: 106759670
VAR: 108332369
CCAJ: 109813775
CAM: 101498546
LJA: Lj0g3v0131669.1(Lj0g3v0131669.1) Lj2g3v3224400.1(Lj2g3v3224400.1)
ADU: 107459807
AIP: 107613512
FVE: 101313434
PPER: 18782019
PAVI: 110765908
CSV: 101221943
CMO: 103501765
MCHA: 111012255
RCU: 8277795
HBR: 110663464
JRE: 109019225
INI: 109150563
SIND: 105165531
HAN: 110885953
LSV: 111904482
CCAV: 112516959
DCR: 108223439
BVG: 104907336
SOE: 110775567
OSA: 4326319
DOSA: Os01t0667200-01(Os01g0667200)
OBR: 102722159
BDI: 100826131
ATS: 109778914(LOC109778914)
SBI: 8060399
ZMA: 100283164(IDP546)
SITA: 101785668
DCT: 110101845
ATR: 18437340
MNG: MNEG_3639
SMIN: v1.2.004789.t1(symbB.v1.2.004789.t1) v1.2.008370.t1(symbB.v1.2.008370.t1) v1.2.017459.t1(symbB.v1.2.017459.t1) v1.2.020192.t1(symbB.v1.2.020192.t1) v1.2.025153.t1(symbB.v1.2.025153.t1)
PTI: PHATRDRAFT_16707(GLO_1)
 » 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 122:22-33 (1966)
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 149:1699-710 (2003)
DOI:10.1099/mic.0.26212-0
Reference
3  [PMID:24389926]
  Authors
Liu H, Xin Y, Xun L
  Title
Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria.
  Journal
Appl Environ Microbiol 80:1799-806 (2014)
DOI:10.1128/AEM.03281-13
Reference
4  [PMID:22786886]
  Authors
Holdorf MM, Owen HA, Lieber SR, Yuan L, Adams N, Dabney-Smith C, Makaroff CA
  Title
Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for embryo and endosperm development.
  Journal
Plant Physiol 160:226-36 (2012)
DOI:10.1104/pp.112.201855
  Sequence
[ath:AT1G53580]
Reference
5  [PMID:25596185]
  Authors
Pettinati I, Brem J, McDonough MA, Schofield CJ
  Title
Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy.
  Journal
Hum Mol Genet 24:2458-69 (2015)
DOI:10.1093/hmg/ddv007
  Sequence
[hsa:23474]
Other DBs
ExplorEnz - The Enzyme Database: 1.13.11.18
IUBMB Enzyme Nomenclature: 1.13.11.18
ExPASy - ENZYME nomenclature database: 1.13.11.18
BRENDA, the Enzyme Database: 1.13.11.18
CAS: 37256-58-9

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