KEGG   ENZYME: 1.8.99.5
Entry
EC 1.8.99.5                 Enzyme                                 
Name
dissimilatory sulfite reductase;
siroheme sulfite reductase;
hydrogen-sulfide:(acceptor) oxidoreductase (ambiguous);
DsrAB
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With unknown physiological acceptors
Sysname
hydrogen-sulfide:[DsrC sulfur-carrier protein],acceptor oxidoreductase
Reaction(IUBMB)
(1) hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+ (overall reaction) [RN:R00861];
(1a) hydrogen sulfide + a [DsrC protein]-disulfide = a [DsrC protein]-S-sulfanyl-L-cysteine;
(1b) a [DsrC protein]-S-sulfanyl-L-cysteine + 2 acceptor + 3 H2O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+;
(2) a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H+ (overall reaction);
(2a) a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = a [DsrC]-S-sulfo-L-cysteine + 3 reduced acceptor + H+;
(2b) a [DsrC]-S-sulfo-L-cysteine = sulfite + a [DsrC protein]-disulfide
Reaction(KEGG)
R00861;
(other) R00295 R08035
Substrate
hydrogen sulfide [CPD:C00283];
[DsrC protein]-disulfide;
acceptor [CPD:C00028];
H2O [CPD:C00001];
[DsrC protein]-S-sulfanyl-L-cysteine;
[DsrC]-S-sulfo-L-cysteine
Product
sulfite [CPD:C00094];
[DsrC protein]-dithiol;
reduced acceptor [CPD:C00030];
H+ [CPD:C00080];
[DsrC protein]-S-sulfanyl-L-cysteine;
[DsrC protein]-disulfide;
[DsrC]-S-sulfo-L-cysteine
Comment
Contain siroheme. The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. In sulfur reducers it catalyses the reduction of sulfite to sulfide (reaction 1 in the right to left direction), while in sulfur oxidizers it catalyses the opposite reaction (reaction 2 in the left to right direction) [1]. The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. During the process an intramolecular disulfide bond is formed between two L-cysteine residues of DsrC. This disulfide can be reduced by a number of proteins including DsrK and TcmB [5]. This enzyme is different from EC 1.8.1.2, assimilatory sulfite reductase (NADPH), and EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin), which are involved in sulfate assimilation.
History
EC 1.8.99.5 created 2015
Pathway
ec00633  Nitrotoluene degradation
ec00920  Sulfur metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K11180  dissimilatory sulfite reductase alpha subunit
K11181  dissimilatory sulfite reductase beta subunit
Genes
TIGTHII_0611 THII_0612
THISHZT40_16500(dsrB) HZT40_16505(dsrA)
TUNJ9260_02800(dsrA) J9260_02805(dsrB)
TLOJ9253_11315(dsrB) J9253_11320(dsrA)
TSBHMY34_03705(dsrB) HMY34_03710(dsrA)
TANIJ8380_00610(dsrB) J8380_00615(dsrA)
TWNL2Y54_11490(dsrA) L2Y54_11495(dsrB)
ALVAlvin_1251(dsrA) Alvin_1252(dsrB)
ATEPAtep_14700(dsrA-2) Atep_14710(dsrB-1)
TVIThivi_0544 Thivi_0545
TMBThimo_0143 Thimo_0144
MPURMARPU_10910 MARPU_10915
TSYTHSYN_22540 THSYN_22545
TTPE6P07_09385(dsrB) E6P07_09390(dsrA)
THIPN838_27035(dsrB) N838_27040(dsrA)
CJAPGWK36_02290(dsrA) GWK36_02295(dsrB)
THIMKFB96_10675(dsrB) KFB96_10680(dsrA)
TBOGLT988_06660(dsrB) LT988_06665(dsrA)
AEHMlg_1653 Mlg_1654
HHAHhal_1951 Hhal_1952
HHKHH1059_16540(dsrA-2) HH1059_16550(dsrB-1)
TGRTgr7_2185 Tgr7_2186
TNITVNIR_0859(dsrB_[H]) TVNIR_0860 TVNIR_1766 TVNIR_1767(dsvB_[H])
TTITHITH_11980 THITH_11985
TTCFOKN1_1306 FOKN1_1307 FOKN1_1945 FOKN1_1946
THICTspCOW1_07090(dsrB-1_1) TspCOW1_07100(dsrA-2_1) TspCOW1_13130(dsrB-1_2) TspCOW1_13140(dsrA-2_2)
TBNTBH_C2461(dsrB) TBH_C2462(dsrA)
EPSL0Y14_12180(dsrB) L0Y14_12185(dsrA)
SLIMSCL_0256 SCL_0257 SCL_1273 SCL_1274
SVASVA_0258 SVA_0259 SVA_1954 SVA_1955
ACIIC4901_06765(dsrA) C4901_06770(dsrB)
ATYA9R16_006355(dsrA) A9R16_006360(dsrB)
SEDSAAY24_10390 AAY24_17300 AAY24_17305
THOSP60_01865 SP60_01870
REVHUE57_11060(dsrB) HUE57_11065(dsrA)
RMARmag_0869 Rmag_0870
REOHUE58_04365(dsrB) HUE58_04370(dsrA)
VOKCOSY_0794(dsrB) COSY_0795(dsrA)
EBHBSEPE_1260(dsrB) BSEPE_1261(dsrA)
BTHGMS2017_1748 MS2017_1749
ENMEBS_1783(dsrB) EBS_1784(dsrA)
IFOCVFO_0512(dsrA) CVFO_0513(dsrB)
APHFCVPH_1070(dsrB) CVPH_1071(dsrA)
RHOBHTY51_04615(dsrB) HTY51_04620(dsrA)
HTNKI616_02630(dsrB) KI616_02635(dsrA)
BBAGE1O_03050 E1O_03060
SHDSUTH_01443(dsrB) SUTH_01444(dsrA)
TBDTbd_1309 Tbd_1369 Tbd_2484 Tbd_2485
SLTSlit_1685 Slit_1686
FAMOYT1_ch1915 OYT1_ch1916
SEMEMIZ01_1475 MIZ01_1476
SDRSCD_n02074(dsrA) SCD_n02717(dsrB) SCD_n02718(dsrA)
SLACSKTS_04680(dsrA-2_1) SKTS_33660(dsrB-1) SKTS_33670(dsrA-2_2)
DDZDSYM_11230 DSYM_11240
RVARvan_0599 Rvan_0600
BLAGBLTE_30830(dsrB-1) BLTE_30840(dsrA-2)
PAMOBAR1_04755(dsrA) BAR1_04760(dsrB)
MAGamb3367 amb3368
MGYMGMSRv2__3911(dsrB) MGMSRv2__3912(dsrA)
MGRYMSR1_25020(dsvA) MSR1_25030(dsvB)
MAGXXM1_4244(dsrA) XM1_4245(dsrB)
MAGNWV31_00295 WV31_00300
MAGQMGMAQ_2110(dsrA) MGMAQ_2111(dsrB)
VSUP3M64_01050(dsrB) P3M64_01055(dsrA)
MGMMmc1_2156 Mmc1_2157
DAVDESACE_07215 DESACE_07220
DVUDVU_0402(dsvA) DVU_0403(dvsB)
DVLDvul_2531 Dvul_2532
DVMDvMF_1553 DvMF_1554
DVGDeval_0364 Deval_0365
DDSDdes_0920 Ddes_0921 Ddes_2294 Ddes_2295
DFIAXF13_14280 AXF13_14285
DPGDESPIGER_1934 DESPIGER_1935 DESPIGER_1939 DESPIGER_1940
DEFCNY67_09565(dsrA) CNY67_09570(dsrB) CNY67_15020(dsrB) CNY67_15025(dsrA)
DTRRSDT_0579(dsrB) RSDT_0580(dsrA)
DFLDFE_3070 DFE_3071
PSYFN1030_11325(dsrA) N1030_11330(dsrB)
DSBLN040_13680(dsrB) LN040_13685(dsrA)
DMADMR_03600 DMR_03610
DCBC3Y92_18590(dsrB) C3Y92_18595(dsrA)
DGGDGI_0689(dsrB) DGI_0691(dsrA)
DDEDde_0526 Dde_0527
DMSE8L03_15015(dsrA) E8L03_15020(dsrB)
DSADesal_0787 Desal_0788
DHYDESAM_20116(dsvB) DESAM_20117(dsvA)
DAFDesaf_1370 Desaf_1371
DASDaes_2984 Daes_2985
DPIBN4_12627(dsrA) BN4_12628(dsrB)
DEJAWY79_17895 AWY79_17900
PPRFDPRO_1445(dsvB) DPRO_1446(dsvA)
PSELGM415_02165(dsrB) GM415_02170(dsrA)
DDNDND132_2809 DND132_2810
PSEFPSDVSF_27400(dsvA) PSDVSF_27410(dsvB)
PPORJCM14722_23130(dsvA) JCM14722_23140(dsvB)
PNWSYK_28400(dsvA) SYK_28410(dsvB)
DSXGD604_02670(dsrA) GD604_02675(dsrB)
DSDGD606_09330(dsrB) GD606_09335(dsrA)
PBIZLWC08_10490(dsrB) LWC08_10495(dsrA)
CLIHKPS_001845(dsrA) KPS_001846(dsrB)
DBADbac_0279 Dbac_0280
DOAAXF15_07380 AXF15_07385
DESUNLA06_11460(dsrB) NLA06_11465(dsrA)
THEWTDMWS_09240(dsvA) TDMWS_09250(dsvB)
DRTDret_0244(dsrA) Dret_0245(dsrB)
DPSDP0797 DP0798
DSFUWK_01633 UWK_01634
DLMDPPLL_01100 DPPLL_01110
DAKDaAHT2_0296 DaAHT2_0297
DPRDespr_2940 Despr_2941
DEOCAY53_04490 CAY53_04495
DOGHP555_06390(dsrA) HP555_06395(dsrB)
DBKDGMP_00400(dsvA) DGMP_00410
DDUGF1_25900 GF1_25910
DOLDole_2669 Dole_2670
DALDalk_4300 Dalk_4301
DATHRM2_42390(dsrB2) HRM2_42400(dsrA2)
DTOTOL2_C05570(dsrA) TOL2_C05580(dsrB)
DOVDSCO28_40940(dsvA) DSCO28_40950(dsvB)
DWDDSCW_41400(dsvA) DSCW_41410(dsvB)
DALKDSCA_41750(dsvB) DSCA_41760(dsvA)
DMLDmul_28170(dsrB) Dmul_28180(dsrA)
DLIdnl_18160(dsrA) dnl_18170(dsrB)
DMMdnm_073370(dsrB) dnm_073380(dsrA)
DEKDSLASN_37970(dsvA) DSLASN_37980(dsvB)
DAODesac_1622 Desac_1623
DTIDesti_1555 Desti_1556
SFUSfum_4042 Sfum_4043
DAXFDQ92_05050(dsrB) FDQ92_05055(dsrA)
DBRDeba_0959 Deba_0960
TIDThein_0404 Thein_0405
TOPTOPB45_1406 TOPB45_1407
TCMHL41_05695
THETF1847_01210(dsrA) F1847_01215(dsrB)
CTHITHC_0449 THC_0450
TAVG4V39_07740(dsrA) G4V39_07745(dsrB)
TMAIFVE67_07900(dsrA) FVE67_07905(dsrB)
DHRLGS26_00980(dsrA) LGS26_00985(dsrB)
DSYDSY0309(dsrA) DSY0310(dsrB)
DHDDhaf_0252 Dhaf_0253
DDHDesde_0266 Desde_0267
DDLDesdi_0242 Desdi_0243
DORDesor_3302 Desor_3303
DAIDesaci_3004 Desaci_3005
DMIDesmer_2566 Desmer_2567
DCADesca_2665 Desca_2666
DRMDred_3186 Dred_3187
DRUDesru_0386 Desru_0387 Desru_3723 Desru_3724
DFGB0537_15840 B0537_15845
DAEDtox_0079 Dtox_0080
DKUDesku_3492 Desku_3493
DAUDaud_2200 Daud_2201
TFRBR63_06745(dsrB) BR63_06750(dsrA)
FWADCMF_23740 DCMF_23745
AACXDEACI_0668 DEACI_0669
DGIDesgi_4661 Desgi_4662
CHYCHY_2409(dsrB) CHY_2410(dsrA)
ADGAdeg_2093 Adeg_2094
TNRThena_1366 Thena_1367
TACITDSAC_1342 TDSAC_1343
MTAMoth_1600 Moth_1601 Moth_1629 Moth_1630
MTHOMOTHE_c15990(dsvB1) MOTHE_c16000(dsvA1) MOTHE_c16350(dsvB2) MOTHE_c16360(dsvA2)
MTHZMOTHA_c16820(dsvB1) MOTHA_c16830(dsvA1) MOTHA_c17180(dsvB2) MOTHA_c17190(dsvA2)
EGDGS424_009590(dsrB) GS424_009595(dsrA)
GPAGPA_16670 GPA_16680
CBACJI75_04655 JI75_04660
CTECT0852(dsrA-1) CT0853(dsrB-1) CT2249(dsrA-2)
CPCCpar_0028 Cpar_0029
CLZBIU88_06835 BIU88_06840 BIU88_11280
CCHCag_1955 Cag_1956
CPHCpha266_0128 Cpha266_0129
CPBCphamn1_1856 Cphamn1_1857
CLIClim_0694 Clim_0695
PVICvib_0039 Cvib_0040
PLTPlut_0036 Plut_0037
PPHPpha_2320 Ppha_2321
PAAPaes_0029 Paes_0030
PROCPtc2401_00028(dsvA) Ptc2401_00029(dsvB)
PRSB9H02_00140
PROSCHL67_00155(dsrA) CHL67_00160(dsrB)
TYETHEYE_A1994(dsrA) THEYE_A1995(dsrB)
DTPJZK55_23470(dsrB) JZK55_23480(dsrA)
AFUAF_0423 AF_0424
AFGAFULGI_00004270 AFULGI_00004280
APOArcpr_0139 Arcpr_0140
AVEArcve_1948 Arcve_1949
ASTAsulf_00915 Asulf_00916
PAIPAE2571 PAE2572 PAE2596 PAE2597
PISPisl_0170 Pisl_0171
PCLPcal_1445 Pcal_1446 Pcal_1456 Pcal_1457
PASPars_0907 Pars_0908 Pars_1212 Pars_1213 Pars_1224
PYRP186_1805 P186_1806 P186_1813 P186_1814
POGPogu_0993 Pogu_0994 Pogu_1014 Pogu_1015 Pogu_1026 Pogu_1027
TNETneu_0344 Tneu_0345
CMACmaq_0853 Cmaq_0854
TTNTTX_0423(dsrA) TTX_0424(dsrA) TTX_0426(dsrA) TTX_0427(dsrA) TTX_1187(dsrB) TTX_1188(dsrA)
VDIVdis_2098 Vdis_2099
VMOVMUT_0501 VMUT_0502
VSOVsou_25600 Vsou_25610
 » show all
Reference
1
  Authors
Schedel, M., Vanselow, M. and Trueper, H. G.
  Title
Siroheme sulfite reductase from Chromatium vinosum. Purification and investigation of some of its molecular and catalytic properties.
  Journal
Arch Microbiol 121:29-36 (1979)
Reference
2  [PMID:7338517]
  Authors
Seki Y, Sogawa N, Ishimoto M
  Title
Siroheme as an active catalyst in sulfite reduction.
  Journal
J Biochem 90:1487-92 (1981)
DOI:10.1093/oxfordjournals.jbchem.a133615
Reference
3  [PMID:9695921]
  Authors
Pott AS, Dahl C
  Title
Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur.
  Journal
Microbiology 144 ( Pt 7):1881-94 (1998)
DOI:10.1099/00221287-144-7-1881
  Sequence
Reference
4  [PMID:18829451]
  Authors
Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M
  Title
The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration.
  Journal
J Biol Chem 283:34141-9 (2008)
DOI:10.1074/jbc.M805643200
Reference
5  [PMID:24662917]
  Authors
Venceslau SS, Stockdreher Y, Dahl C, Pereira IA
  Title
The "bacterial heterodisulfide" DsrC is a key protein in dissimilatory sulfur metabolism.
  Journal
Biochim Biophys Acta 1837:1148-64 (2014)
DOI:10.1016/j.bbabio.2014.03.007
Other DBs
ExplorEnz - The Enzyme Database: 1.8.99.5
IUBMB Enzyme Nomenclature: 1.8.99.5
ExPASy - ENZYME nomenclature database: 1.8.99.5
BRENDA, the Enzyme Database: 1.8.99.5
CAS: 37256-51-2

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