KEGG   ENZYME: 1.8.2.2Help
Entry
EC 1.8.2.2                  Enzyme                                 

Name
thiosulfate dehydrogenase;
tsdA (gene name);
tetrathionate synthase;
thiosulfate oxidase;
thiosulfate-oxidizing enzyme;
thiosulfate-acceptor oxidoreductase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With a cytochrome as acceptor
BRITE hierarchy
Sysname
thiosulfate:ferricytochrome-c oxidoreductase
Reaction(IUBMB)
2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c [RN:R00029]
Reaction(KEGG)
Substrate
thiosulfate [CPD:C00320];
ferricytochrome c [CPD:C00125]
Product
tetrathionate [CPD:C02084];
ferrocytochrome c [CPD:C00126]
Comment
The enzyme catalyses the reversible formation of a sulfur-sulfur bond between the sulfane atoms of two thiosulfate molecules, yielding tetrathionate and releasing two electrons. In many bacterial species the enzyme is a diheme c-type cytochrome. In a number of organisms, including Thiomonas intermedia and Sideroxydans lithotrophicus, a second diheme cytochrome (TsdB) acts as the electron acceptor. However, some organisms, such as Allochromatium vinosum, lack TsdB. The electron acceptor in these organisms may be the high-potential iron-sulfur protein (HiPIP).
History
EC 1.8.2.2 created 1990
Orthology
K19713  thiosulfate dehydrogenase
Genes
PFQ: QQ39_10585
XCV: XCV2384
SML: Smlt1757
SMT: Smal_1496
BUJ: BurJV3_1545
SMZ: SMD_1692
STEN: CCR98_08195
STEM: CLM74_08445
DTX: ATSB10_01860
VPA: VP2016
VPB: VPBB_1852
VAG: N646_1094
PAEO: M801_4586
PPU: PP_3822
PPF: Pput_1948
PPT: PPS_3304
PPI: YSA_09265
PPX: T1E_1482
PPUH: B479_16450
PPUT: L483_21430
PPUN: PP4_18600
PPUD: DW66_3733
PMON: X969_15935
PMOT: X970_15580
PFS: PFLU_2981
PEN: PSEEN2293
PSA: PST_2843
PSEM: TO66_17620
PSIL: PMA3_13520
PAR: Psyc_1943
SON: SO_4047
SFR: Sfri_3545
SAZ: Sama_0527
SLO: Shew_0524
SWP: swp_4554
SPSW: Sps_02951
PSM: PSM_A1193
MAQ: Maqu_1184
MHC: MARHY2080
PIN: Ping_1309
NWA: Nwat_0737
TEE: Tel_05960
NTT: TAO_1755
TVR: TVD_02035
HAM: HALO3279
AXE: P40_06455
OCE: GU3_00620
LHK: LHK_00203
BPS: BPSS1729
BPSE: BDL_5085
BPSM: BBQ_4410
BPSU: BBN_5185
BPSD: BBX_4251
BPK: BBK_4449
BPSH: DR55_3538
BPSA: BBU_4295
BPSO: X996_5815
BUT: X994_5376
BTZ: BTL_3445
BTD: BTI_4240
BTHA: DR62_5609
BVE: AK36_3912
BCJ: BCAM2443
BCEN: DM39_5393
BCEO: I35_6343
BAM: Bamb_4606
BCT: GEM_3234
BCED: DM42_5538
BCON: NL30_00350
BPSL: WS57_01890
BUL: BW21_3780
BPE: BP1579
BPC: BPTD_1561
BPER: BN118_1841
BPET: B1917_1502
BPEU: Q425_17590
BPA: BPP3004
BPAR: BN117_2704
BBR: BB2970
BAV: BAV1806
TEA: KUI_1261
BPSI: IX83_02985
AFQ: AFA_06400
PNA: Pnap_2825
AJS: Ajs_1415
CTES: O987_15870
RGE: RGE_28840
TBD: Tbd_0128
SLT: Slit_1878
EBA: ebA618(cytC5)
DAR: Daro_2492
AZO: azo2669
AOA: dqs_2815
TCL: Tchl_2725
WSU: WS0009(CYTA)
CJU: C8J_0815
CJM: CJM1_0842
CJEJ: N564_00845
CJEU: N565_00889
CJEN: N755_00886
CJEI: N135_00914
CJY: QZ67_00940(soxA)
CJQ: UC78_0830
CCV: CCV52592_0286(tsdA)
CGRA: CGRAC_1216
CSPF: CSF_1415(tsdA)
ABU: Abu_0902
ABT: ABED_0851
ARC: ABLL_1136
SDL: Sdel_0259
SMUL: SMUL_0337
SHAL: SHALO_0303
SULJ: SJPD1_0302
ADE: Adeh_1278
MXA: MXAN_7047
CCX: COCOR_00358(qcrC)
SMER: DU99_20775
BME: BMEII0895
BMEL: DK63_2353
BMEE: DK62_3055
BMF: BAB2_0850
BABO: DK55_2806
BABR: DO74_2120
BABT: DK49_2434
BABB: DK48_2991
BABU: DK53_2808
BABS: DK51_2293
BABC: DO78_2249
BMS: BRA0353
BSZ: DK67_2359
BOV: BOV_A0320
BCAR: DK60_2079
BCAS: DA85_12160
BMR: BMI_II348
BPP: BPI_II351
BPV: DK65_2135
OAN: Oant_0690
OAH: DR92_2251
RPA: RPA2003
RPB: RPB_3370
RPD: RPD_2072
RPT: Rpal_2214
NHA: Nham_0193
AZC: AZC_4146
MSL: Msil_1092
HDN: Hden_2748
MSC: BN69_0022
MCG: GL4_2534
BLAS: BSY18_1358
LSP: Bsph_4408
VPN: A21D_02821(soxA)
BTS: Btus_0272
PCU: pc0909
PNL: PNK_1194
PUV: PUV_11070
WCH: wcw_0515
RBA: RB11269
PBOR: BSF38_03380(tsdA)
ACA: ACP_0532
GBA: J421_1806
CPI: Cpin_2599
MUC: MuYL_3266
FJG: BB050_00265(petJ)
HTH: HTH_1461
NDE: NIDE3886
NMO: Nmlp_3213
 » show all
Taxonomy
Reference
1
  Authors
Lu, W.-P. and Kelly, D.P.
  Title
Cellular location and partial purification of the 'thiosulphate-oxidizing enzyme' and 'trithionate hydrolase' from Thiobacillus tepidarius.
  Journal
J Gen Microbiol 134:877-885 (1988)
Reference
2
  Authors
Fukumori, Y. and Yamanaka, T.
  Title
A high-potential nonheme iron protein (HiPIP)-linked, thiosulfate-oxidizing enzyme derived from Chromatium vinosum.
  Journal
Curr Microbiol 3:117-120 (1979)
Reference
3  [PMID:23421726]
  Authors
Liu YW, Denkmann K, Kosciow K, Dahl C, Kelly DJ
  Title
Tetrathionate stimulated growth of Campylobacter jejuni identifies a new type of  bi-functional tetrathionate reductase (TsdA) that is widely distributed in bacteria.
  Journal
Mol Microbiol 88:173-88 (2013)
DOI:10.1111/mmi.12176
Reference
4  [PMID:25673691]
  Authors
Brito JA, Denkmann K, Pereira IA, Archer M, Dahl C
  Title
Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum: structural and functional insights into thiosulfate oxidation.
  Journal
J Biol Chem 290:9222-38 (2015)
DOI:10.1074/jbc.M114.623397
Reference
5  [PMID:27694441]
  Authors
Kurth JM, Brito JA, Reuter J, Flegler A, Koch T, Franke T, Klein EM, Rowe SF, Butt JN, Denkmann K, Pereira IA, Archer M, Dahl C
  Title
Electron Accepting Units of the Diheme Cytochrome c TsdA, a Bifunctional Thiosulfate Dehydrogenase/Tetrathionate Reductase.
  Journal
J Biol Chem 291:24804-24818 (2016)
DOI:10.1074/jbc.M116.753863
Other DBs
ExplorEnz - The Enzyme Database: 1.8.2.2
IUBMB Enzyme Nomenclature: 1.8.2.2
ExPASy - ENZYME nomenclature database: 1.8.2.2
BRENDA, the Enzyme Database: 1.8.2.2
CAS: 9076-88-4

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