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Entry
EC 2.8.5.2                  Enzyme                                 

Name
L-cysteine S-thiosulfotransferase;
SoxXA;
thiosulfate:[SoxY protein]-L-cysteine thiosulfotransferase
Class
Transferases;
Transferring sulfur-containing groups;
Thiosulfotransferases
BRITE hierarchy
Sysname
thiosulfate:[SoxY protein]-L-cysteine thiosulfonotransferase
Reaction(IUBMB)
(1) [SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+ [RN:R12163];
(2) [SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+ [RN:R12164]
Reaction(KEGG)
Substrate
[SoxY protein]-L-cysteine [CPD:C21972];
thiosulfate [CPD:C00320];
ferricytochrome c [CPD:C00125];
[SoxY protein]-S-sulfanyl-L-cysteine [CPD:C21898]
Product
[SoxY protein]-S-sulfosulfanyl-L-cysteine [CPD:C21815];
ferrocytochrome c [CPD:C00126];
H+ [CPD:C00080];
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine [CPD:C21899]
Comment
The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. It catalyses two reactions in the pathway - early in the pathway it attaches a thiosulfate molecule to the sulfur atom of an L-cysteine of a SoxY protein; later it transfers a second thiosulfate molecule to a sulfane group that is already attached to the same cysteine residue.
History
EC 2.8.5.2 created 2018
Pathway
ec00920  Sulfur metabolism
Orthology
K17222  L-cysteine S-thiosulfotransferase
K17223  L-cysteine S-thiosulfotransferase
Genes
MSQ: BKP64_06045 BKP64_06060
MAH: MEALZ_1026 MEALZ_1318(soxA)
TCX: Tcr_0601 Tcr_0604
HTR: EPV75_03655(soxA) EPV75_03670(soxX) EPV75_10970(soxX) EPV75_10980(soxA)
TCY: Thicy_0216 Thicy_0219
TAO: THIAE_01265 THIAE_01280
THIO: AYJ59_10135 AYJ59_10150
TIG: THII_1580
BLEP: AL038_11110
ALV: Alvin_2168(soxX) Alvin_2169(soxA)
HHA: Hhal_1948
RFO: REIFOR_02318(soxX) REIFOR_02321(soxA)
ACII: C4901_13015(soxX) C4901_13030(soxA)
TBN: TBH_C2346(soxX) TBH_C2347(soxA)
VOK: COSY_0730(soxA) COSY_0733(soxX)
EBH: BSEPE_0441(soxX) BSEPE_0444(soxA)
ENM: EBS_1635(soxX) EBS_1638(soxA)
RSE: F504_3296(soxX) F504_3297(soxA)
RPU: CDC45_16645(soxX) CDC45_16650(soxA)
REH: H16_A3565(soxX) H16_A3566(soxA)
CNC: CNE_1c35150(soxX) CNE_1c35160(soxA)
RME: Rmet_3419(soxX) Rmet_3420(soxA)
CPAU: EHF44_06310(soxA) EHF44_06315(soxX)
POH: DPM16_03920(soxA) DPM16_03925(soxX) DPM16_05465(soxA) DPM16_05480(soxX)
POS: DT070_18145(soxX) DT070_18150(soxA) DT070_18420(soxX) DT070_18435(soxA)
VBO: CKY39_30920(soxX) CKY39_30925(soxA)
HYR: BSY239_836(soxA) BSY239_837(soxX)
MELA: C6568_08780(soxX) C6568_08785(soxA)
METP: C1M51_15785(soxX) C1M51_15790(soxA)
MMS: mma_0451(soxA) mma_0452
MASZ: C9I28_00070(soxA) C9I28_00085(soxX)
MASY: DPH57_21585(soxX) DPH57_21600(soxA)
PBH: AAW51_2270(soxA) AAW51_2271(soxX)
SHD: SUTH_02728(soxA) SUTH_02729(soxX) SUTH_03438(soxX) SUTH_03439(soxA)
METR: BSY238_1524(soxA) BSY238_1525(soxX)
SDR: SCD_n02409(soxA) SCD_n02412(soxX)
DEY: HYN24_04375(soxA) HYN24_04380(soxX)
ATW: C0099_11260(soxX) C0099_11265(soxA)
ACOM: CEW83_09805(soxX) CEW83_09810(soxA)
ABU: Abu_0567(soxX) Abu_0570(soxA)
ASK: EI285_02185(soxX) EI285_02200(soxA)
AHS: AHALO_0637(soxX) AHALO_0640(soxA)
AGC: BSY240_3513(soxX) BSY240_3516(soxA)
RHT: NT26_2614(soxA) NT26_2617(soxX)
BJA: bll1011(soxA) bll1014(soxX) bll2732 blr3511(soxX) blr3514(soxA)
BRK: CWS35_09090(soxA) CWS35_09105(soxX) CWS35_16995(soxA) CWS35_17010(soxX)
BOT: CIT37_09230(soxX) CIT37_09245(soxA) CIT37_36645(soxA) CIT37_36660(soxX) CIT37_39940(soxX) CIT37_39955(soxA)
BRQ: CIT40_08120(soxA) CIT40_08135(soxX) CIT40_11160(soxX) CIT40_11175(soxA) CIT40_30390(soxX) CIT40_30405(soxA)
BOS: BSY19_747(soxX) BSY19_748(soxA) BSY19_936(soxX) BSY19_939(soxA)
MEA: Mex_1p2562(soxX) Mex_1p2565(soxA)
MDI: METDI0756(soxA) METDI0759(soxX)
MEE: DA075_23825(soxA) DA075_30085(soxX)
METD: C0214_09180(soxX) C0214_09195(soxA)
DEQ: XM25_01325(SoxX) XM25_01340(SoxA)
BRN: D1F64_10940(soxX) D1F64_10955(soxA)
SIL: SPO0993(soxX) SPO0996(soxA)
RUA: D1823_09095(soxA) D1823_09110(soxX)
RDE: RD1_1511(soxX) RD1_1514(soxA)
RLI: RLO149_c031850(soxA1) RLO149_c031880(soxX)
PARU: CYR75_11895(soxX) CYR75_11910(soxA)
PARS: DRW48_07260(soxX) DRW48_07275(soxA)
DSH: Dshi_2804(soxA1) Dshi_2807
PSF: PSE_1364(soxA) PSE_1367(soxX)
PGA: PGA1_c12420(soxX) PGA1_c12450(soxA2)
PGL: PGA2_c12400(soxX) PGA2_c12430(soxA2)
PHP: PhaeoP97_01238(soxX) PhaeoP97_01241(soxA2)
PPIC: PhaeoP14_01161(soxX) PhaeoP14_01164(soxA2)
PHQ: D1820_02240(soxX) D1820_02255(soxA)
OTM: OSB_13190 OSB_13220(soxA)
LEJ: ETW24_08435(soxX) ETW24_08450(soxA)
PTP: RCA23_c17380(soxA2) RCA23_c17410(soxX)
CEH: CEW89_07115(soxA) CEW89_07130(soxX)
RSU: NHU_02677(soxA) NHU_02680(soxX)
LABR: CHH27_14095(soxX) CHH27_14110(soxA)
YPAC: CEW88_16495(soxA) CEW88_16510(soxX)
SULZ: C1J03_15090(soxA) C1J03_15105(soxX)
SULI: C1J05_07870(soxX) C1J05_07885(soxA)
RBG: BG454_05035(soxA) BG454_05050(soxX)
SAGU: CDO87_03830(soxA) CDO87_03845(soxX)
THAS: C6Y53_05085(soxX) C6Y53_05100(soxA)
SALO: EF888_14350(soxA) EF888_14365(soxX)
SEDI: EBB79_03295(soxX) EBB79_03310(soxA)
MGRY: MSR1_20790 MSR1_20820(soxA)
TII: DY252_12655(soxA) DY252_12670(soxX)
MAGQ: MGMAQ_1861(soxA) MGMAQ_1864(soxX)
PHR: C6569_04485(soxA) C6569_04500(soxX) C6569_08430(soxX) C6569_08435(soxA)
HTL: HPTL_0813(soxA) HPTL_0814(soxX)
TSC: TSC_c21050(soxA1) TSC_c21060(soxX) TSC_c21080 TSC_c21090(soxA2)
CTE: CT1016(soxX) CT1019(soxA)
HTH: HTH_1517(soxA1) HTH_1518(soxA2) HTH_1519(soxX)
 » show all
Taxonomy
Reference
1  [PMID:10940005]
  Authors
Friedrich CG, Quentmeier A, Bardischewsky F, Rother D, Kraft R, Kostka S, Prinz H
  Title
Novel genes coding for lithotrophic sulfur oxidation of Paracoccus pantotrophus GB17.
  Journal
J Bacteriol 182:4677-87 (2000)
DOI:10.1128/JB.182.17.4677-4687.2000
  Sequence
Reference
2  [PMID:11523998]
  Authors
Cheesman MR, Little PJ, Berks BC
  Title
Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum.
  Journal
Biochemistry 40:10562-9 (2001)
DOI:10.1021/bi0100081
Reference
3  [PMID:12147345]
  Authors
Rother D, Friedrich CG
  Title
The cytochrome complex SoxXA of Paracoccus pantotrophus is produced in Escherichia coli and functional in the reconstituted sulfur-oxidizing enzyme system.
  Journal
Biochim Biophys Acta 1598:65-73 (2002)
Reference
4  [PMID:12411478]
  Authors
Bamford VA, Bruno S, Rasmussen T, Appia-Ayme C, Cheesman MR, Berks BC, Hemmings AM
  Title
Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme.
  Journal
EMBO J 21:5599-610 (2002)
DOI:10.1093/emboj/cdf566
Reference
5  [PMID:16297640]
  Authors
Dambe T, Quentmeier A, Rother D, Friedrich C, Scheidig AJ
  Title
Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation.
  Journal
J Struct Biol 152:229-34 (2005)
DOI:10.1016/j.jsb.2005.09.002
Reference
6  [PMID:16995898]
  Authors
Hensen D, Sperling D, Truper HG, Brune DC, Dahl C
  Title
Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum.
  Journal
Mol Microbiol 62:794-810 (2006)
DOI:10.1111/j.1365-2958.2006.05408.x
Reference
7  [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: 2.8.5.2
IUBMB Enzyme Nomenclature: 2.8.5.2
ExPASy - ENZYME nomenclature database: 2.8.5.2
BRENDA, the Enzyme Database: 2.8.5.2

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