Entry
Name
sulfhydrogenase;
sulfur reductase
Class
Oxidoreductases;
Acting on hydrogen as donor;
With other, known, physiological acceptors
BRITE hierarchy
Sysname
H2:polysulfide oxidoreductase
Reaction(IUBMB)
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1 [RN:
R10390 ]
Reaction(KEGG)
Substrate
Product
hydrogen sulfide [CPD:
C00283 ];
(sulfide)n-1
Comment
An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the beta and gamma subunits function as sulfur reductase and the alpha and delta subunits function as hydrogenases (EC
1.12.1.3 , hydrogen dehydrogenase [NADP+] and EC
1.12.1.4 , hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate [2].
History
EC 1.12.98.4 created 1992 as EC 1.97.1.3, transferred 2013 to EC 1.12.98.4
Pathway
ec01120 Microbial metabolism in diverse environments
Orthology
K17995 sulfhydrogenase subunit gamma (sulfur reductase)
K17996 sulfhydrogenase subunit beta (sulfur reductase)
Genes
THIM : KFB96_22630 KFB96_22635
HHC : M911_03930 M911_03935
TNI : TVNIR_2171(asrB_[H]) TVNIR_2172(asrA_[H])
TTI : THITH_06465 THITH_06470
APRS : BI364_04830 BI364_04835
HSI : BOX17_10630 BOX17_10635
MGEO : CFI10_06210 CFI10_06215
CHIZ : HQ393_09260 HQ393_09265
CFON : HZU75_11935 HZU75_11940
SLAC : SKTS_06270(hdrE) SKTS_06280
GPI : GPICK_06780 GPICK_15715
GBN : GEOBRER4_00240(hdrF) GEOBRER4_17920
GER : KP004_08755 KP004_19720
GSUB : KP001_06405 KP001_16595
GNT : KP003_08280 KP003_19710
DVG : Deval_2220 Deval_2221
DSD : GD606_00165 GD606_07830 GD606_07835 GD606_13020
DCB : C3Y92_00580 C3Y92_00585
DGG : DGI_1053(floxB) DGI_1054(floxA)
DDE : Dde_1213 Dde_3529 Dde_3530
DMS : E8L03_07155 E8L03_12035
DHY : DESAM_21326 DESAM_21327
DAF : Desaf_2136 Desaf_2877
PSEL : GM415_09650 GM415_09655
DSX : GD604_00275 GD604_05905 GD604_05910
DOA : AXF15_11180 AXF15_11185
DRT : Dret_0192 Dret_0193 Dret_2311 Dret_2312
DTO : TOL2_C24210(asrA1) TOL2_C24220(asrB1) TOL2_C28790(asrA2) TOL2_C28800(asrB2)
DOV : DSCO28_27850(hdrF_1) DSCO28_36110(hdrF_2)
DWD : DSCW_47560(hydB-2_1) DSCW_47570(hdrF_1) DSCW_60910(hdrF_2) DSCW_60920(hydB-2_2)
DALK : DSCA_35360 DSCA_54470(hdrF) DSCA_54480(hydB-2)
DMM : dnm_084940(pyrK1) dnm_084960
DAX : FDQ92_05240 FDQ92_05245
BLAG : BLTE_14890 BLTE_14900
CEU : A7L45_12250 A7L45_12255
CTHD : CDO33_09935 CDO33_09940
SMAN : C12CBH8_20580 C12CBH8_20590
BYL : A4V09_16695 A4V09_16700
BPRO : PMF13cell1_01675(asrA_1) PMF13cell1_01676(asrB_1)
BLAB : EYS05_14065 EYS05_14070
DAI : Desaci_2626 Desaci_2627
DMI : Desmer_2225 Desmer_2226
DCA : Desca_0133 Desca_0134 Desca_0139 Desca_0140
DRM : Dred_0140 Dred_0141 Dred_0147 Dred_0148
DRU : Desru_0209 Desru_0210 Desru_0216 Desru_0217
DFG : B0537_01505 B0537_01510 B0537_01540 B0537_01545 B0537_08750 B0537_08755
DAE : Dtox_1281 Dtox_1356 Dtox_1357
DKU : Desku_1430 Desku_1480 Desku_1481
TFR : BR63_02790 BR63_09655 BR63_09660
FWA : DCMF_24640 DCMF_24645
TJR : TherJR_0671 TherJR_0672 TherJR_0941 TherJR_1949 TherJR_1950
DGI : Desgi_2042 Desgi_2043
CMIU : B1H56_01500 B1H56_01505
VPY : HZI73_20450 HZI73_20455
MTHO : MOTHE_c07600(asrA1)
MTHZ : MOTHA_c08540(asrA1)
MAS : Mahau_0898 Mahau_0899
ABAT : CFX1CAM_1230 CFX1CAM_1231
LCRE : Pla8534_67830(asrA)
ALUS : STSP2_01454(asrB) STSP2_01455(asrA)
VAI : BU251_07800 BU251_07805
TSU : Tresu_1319 Tresu_1320
TBE : Trebr_2030 Trebr_2031
TRC : DYE49_06660 DYE49_06665
FVA : FV113G1_17780(asrB) FV113G1_17790(asrA)
FUL : C4N20_13340 C4N20_13345
BOA : Bovatus_04661(asrA) Bovatus_04662(asrB)
BCEL : BcellWH2_01246(asrB) BcellWH2_01247(asrA)
DYS : G7050_05275 G7050_05280
ALD : GFH31_00890 GFH31_00895
CPC : Cpar_0320 Cpar_0945 Cpar_0946
CLZ : BIU88_04770 BIU88_10280 BIU88_10285
CPH : Cpha266_1256 Cpha266_2166
CLI : Clim_1196 Clim_1197 Clim_2094
PROC : Ptc2401_02006(asrA) Ptc2401_02007(asrB)
PRS : B9H02_09665 B9H02_09670
PROS : CHL67_10245 CHL67_10250
DTP : JZK55_04730 JZK55_23580
AVE : Arcve_2105 Arcve_2106
AST : Asulf_01819 Asulf_01820
PFU : PF0891 PF0892 PF1329 PF1330
PFI : PFC_03665 PFC_03670 PFC_05860 PFC_05865
PHO : PH1290(PH1290) PH1291(PH1291)
PAB : PAB0638(hydB-2) PAB0639(hydG-2) PAB1784 PAB1785
PYN : PNA2_1554 PNA2_1555 PNA2_1667 PNA2_1668
PYA : PYCH_00020 PYCH_00030 PYCH_08390 PYCH_08400
PYS : Py04_0890 Py04_0891 Py04_1131 Py04_1132
PYC : TQ32_02775 TQ32_02780 TQ32_03125 TQ32_03130
TON : TON_0054 TON_0055 TON_0536 TON_0537
TSI : TSIB_0282 TSIB_0283 TSIB_1520 TSIB_1521
TBA : TERMP_00067 TERMP_00068 TERMP_00538 TERMP_00539
THE : GQS_02460 GQS_02465 GQS_04975 GQS_04980
THA : TAM4_114 TAM4_307 TAM4_579 TAM4_858
THM : CL1_0141 CL1_0142 CL1_0641 CL1_0642
TLT : OCC_03052 OCC_03057 OCC_12226 OCC_12231
TNU : BD01_0439 BD01_0440 BD01_2065 BD01_2066
TGY : X802_03235 X802_03240 X802_07570 X802_07575
THV : ADU37_CDS02150 ADU37_CDS02160 ADU37_CDS16300 ADU37_CDS16310
TCH : CHITON_0947 CHITON_0948 CHITON_1017 CHITON_1018
TPEP : A0127_05285 A0127_05290 A0127_07145 A0127_07150
TPIE : A7C91_06195 A7C91_06200 A7C91_08735 A7C91_08740
TGG : A3K92_08490 A3K92_08495
TCE : A3L02_00955 A3L02_00960 A3L02_02375 A3L02_02380
TBS : A3L01_00930 A3L01_00935 A3L01_03425 A3L01_03430
THH : CDI07_00930 CDI07_00935 CDI07_03365 CDI07_03370
TSL : A3L11_04685 A3L11_04690 A3L11_07385 A3L11_07390
TTD : A3L14_02385 A3L14_02390 A3L14_05110 A3L14_05115
TPRF : A3L09_05675 A3L09_05680 A3L09_05730 A3L09_05735
TRL : A3L10_03140 A3L10_03145 A3L10_05625 A3L10_05630
TPAF : A3L08_06490 A3L08_06495
THY : A3L12_05470 A3L12_05475
TIC : FH039_02785 FH039_02790 FH039_05980 FH039_05985
TCQ : TIRI35C_0408(shyC) TIRI35C_0409(shyB) TIRI35C_0920(hydG) TIRI35C_0921(hydB)
THEM : FPV09_03365 FPV09_03370 FPV09_06565 FPV09_06570
PPAC : PAP_01500 PAP_01505 PAP_03240 PAP_03245
HDF : AArcSl_2418 AArcSl_2419
BARB : AOA66_1501(shyB) AOA66_1502(shyC_1)
LOKI : Lokiarch_42540(shyB)
PSYT : DSAG12_03222(shyC_2) DSAG12_03717(hydG) DSAG12_03718(shyB)
» show all
Taxonomy
Reference
1
Authors
Zophel, A., Kennedy, M.C., Beinert, H. and Kroneck, P.M.H.
Title
Investigations on microbial sulfur respiration. 1. Activation and reduction of elemental sulfur in several strains of Eubacteria.
Journal
Arch Microbiol 150:72-77 (1988)
Reference
Authors
Ma K, Schicho RN, Kelly RM, Adams MW
Title
Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor.
Journal
Sequence
Reference
3
Authors
Ma, K., Zhou, Z.H. and Adams, M.W.
Title
Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH.
Journal
FEMS Microbiol Lett 122:245-250 (1994)
Reference
Authors
Ma K, Weiss R, Adams MW
Title
Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction.
Journal
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 1.12.98.4
LinkDB
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