KEGG   ENZYME: 1.8.2.6
Entry
EC 1.8.2.6                  Enzyme                                 

Name
S-disulfanyl-L-cysteine oxidoreductase;
SoxCD;
sulfur dehydrogenase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With a cytochrome as acceptor
Sysname
[SoxY protein]-S-disulfanyl-L-cysteine:cytochrome-c oxidoreductase
Reaction(IUBMB)
[SoxY protein]-S-disulfanyl-L-cysteine + 6 ferricytochrome c + 3 H2O = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 6 ferrocytochrome c + 6 H+ [RN:R11971]
Reaction(KEGG)
R11971
Substrate
[SoxY protein]-S-disulfanyl-L-cysteine [CPD:C21814];
ferricytochrome c [CPD:C00125];
H2O [CPD:C00001]
Product
[SoxY protein]-S-sulfosulfanyl-L-cysteine [CPD:C21815];
ferrocytochrome c [CPD:C00126];
H+ [CPD:C00080]
Comment
The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. The enzyme from the bacterium Paracoccus pantotrophus contains a molybdoprotein component and a diheme c-type cytochrome component. The enzyme successively oxidizes the outer sulfur atom in [SoxY protein]-S-disulfanyl-L-cysteine, using three water molecules and forming [SoxY protein]-S-sulfosulfanyl-L-cysteine. During the process, six electrons are transferred to the electron chain via cytochrome c.
History
EC 1.8.2.6 created 2018
Pathway
ec00920  Sulfur metabolism
Orthology
K22622  S-disulfanyl-L-cysteine oxidoreductase SoxD
Genes
LYJ: FKV23_07985
PBC: CD58_18895
MSQ: BKP64_06065
MARA: D0851_07305
KIM: G3T16_11190
METU: GNH96_09145
MAH: MEALZ_1454
MBUR: EQU24_13355
MMAI: sS8_0589
MMOB: F6R98_06955
TCX: Tcr_0157
TEE: Tel_16370
RFO: REIFOR_02317(soxD)
REH: H16_A3571(soxD) H16_B2221(h16_B2221)
RME: Rmet_6117(copJ)
CGD: CR3_2733
BTD: BTI_5283
BCN: Bcen_1239
BCJ: BCAS0417
BCEO: I35_7459
BCT: GEM_4759
BCED: DM42_6978
BSEM: WJ12_18430
BGO: BM43_5313
BUL: BW21_4932
BPH: Bphy_7231
BFN: OI25_51
PNU: Pnuc_0802
PPNO: DA70_17185
PPNM: LV28_13565
PPUL: RO07_07505
PSPU: NA29_03385
PAPI: SG18_07945
LMIR: NCTC12852_01955(cyt)
BPAR: BN117_2482
BPA: BPP1578
BBR: BB2656
BPT: Bpet4582
POL: Bpro_2630
ACRA: BSY15_3141
CTES: O987_17365
RTA: Rta_13790
HYB: Q5W_03640
HPSE: HPF_06270(cyt)
MMS: mma_0447
LCH: Lcho_3783
TIN: Tint_2299
THI: THI_2672
SLT: Slit_0645
NIM: W01_26030
DAR: Daro_3133
AZA: AZKH_3911
BPRC: D521_0984
SUA: Saut_2097
SULC: CVO_09760
ABU: Abu_0566(soxD)
AHS: AHALO_0636(soxD)
AMAR: AMRN_0696(soxD)
ATP: ATR_1125(soxD)
ACAA: ACAN_0716(soxD)
AELL: AELL_0707(soxD)
AAQI: AAQM_0613(soxD)
APOC: APORC_1664(soxD)
HBV: ABIV_1384(soxD)
HEBR: AEBR_1634(soxD)
PACO: AACT_0810(soxD)
ARC: ABLL_0687
SHAL: SHALO_2481
SUN: SUN_0050
ADE: Adeh_2285
MES: Meso_2891
AGC: BSY240_3519(soxD)
RHT: NT26_2611(soxD)
BJA: bll6120 blr3517(soxD)
BRA: BRADO3185
BRS: S23_18010
AOL: S58_14060 S58_44010(soxD)
RPA: RPA4463
RPB: RPB_4367
RPD: RPD_4251
RPE: RPE_3071
RPT: Rpal_4956
NWI: Nwi_2987
NHA: Nham_1094
OCA: OCAR_5181
BOS: BSY19_753
XAU: Xaut_1517
AZC: AZC_3166
SNO: Snov_0967
MEX: Mext_3340
MCH: Mchl_3665
MPO: Mpop_4162
MET: M446_0147
MNO: Mnod_8678
META: Y590_17320
HDN: Hden_1145
BLAG: BLTE_06850(soxD)
HDI: HDIA_3887
SIL: SPO0999(soxD)
RDE: RD1_1517(soxD)
RLI: RLO149_c031820(soxD4)
PDE: Pden_4156
PSF: PSE_1361(soxD) PSE_3088
PGA: PGA1_c12480(soxD2)
PGL: PGA2_c12460(soxD2)
PGD: Gal_02157
PHP: PhaeoP97_01244(soxD2)
PPIC: PhaeoP14_01167(soxD2)
OTM: OSB_13250
PTP: RCA23_c17350(soxD2)
MALG: MALG_03480
RSU: NHU_02674(soxD)
RHC: RGUI_3431
MALU: KU6B_10820
SPHI: TS85_14125
SINB: SIDU_17655
GXL: H845_1325
ASZ: ASN_973
MGRY: MSR1_10470(petJ)
HTL: HPTL_0810(soxD)
DFC: DFI_15365
TRA: Trad_2909
TTH: TT_C1045
TTJ: TTHA1410
TAQ: TO73_0522
MRB: Mrub_2868
ABAS: ACPOL_1925
SUS: Acid_2558
GAU: GAU_2319
CPI: Cpin_0341
CHU: CHU_0560(soxD)
DFE: Dfer_1616
SLI: Slin_2734
FAE: FAES_1991
NJA: NSJP_3283
 » show all
Reference
1  [PMID:11425697]
  Authors
Friedrich CG, Rother D, Bardischewsky F, Quentmeier A, Fischer J
  Title
Oxidation of reduced inorganic sulfur compounds by bacteria: emergence of a common mechanism?
  Journal
Appl Environ Microbiol 67:2873-82 (2001)
DOI:10.1128/AEM.67.7.2873-2882.2001
Reference
2  [PMID:15865447]
  Authors
Bardischewsky F, Quentmeier A, Rother D, Hellwig P, Kostka S, Friedrich CG
  Title
Sulfur dehydrogenase of Paracoccus pantotrophus: the heme-2 domain of the molybdoprotein cytochrome c complex is dispensable for catalytic activity.
  Journal
Biochemistry 44:7024-34 (2005)
DOI:10.1021/bi047334b
Reference
3  [PMID:28257465]
  Authors
Grabarczyk DB, Berks BC
  Title
Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ.
  Journal
PLoS One 12:e0173395 (2017)
DOI:10.1371/journal.pone.0173395
Other DBs
ExplorEnz - The Enzyme Database: 1.8.2.6
IUBMB Enzyme Nomenclature: 1.8.2.6
ExPASy - ENZYME nomenclature database: 1.8.2.6
BRENDA, the Enzyme Database: 1.8.2.6
LinkDB

DBGET integrated database retrieval system