KEGG   ORTHOLOGY: K17995
Entry
K17995                      KO                                     
Symbol
hydG
Name
sulfhydrogenase subunit gamma (sulfur reductase) [EC:1.12.98.4]
Pathway
map00920  Sulfur metabolism
map01120  Microbial metabolism in diverse environments
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09102 Energy metabolism
   00920 Sulfur metabolism
    K17995  hydG; sulfhydrogenase subunit gamma (sulfur reductase)
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.12  Acting on hydrogen as donor
   1.12.98  With other, known, physiological acceptors
    1.12.98.4  sulfhydrogenase
     K17995  hydG; sulfhydrogenase subunit gamma (sulfur reductase)
Other DBs
RN: R10390
Genes
PLAL: FXN65_14060
THIM: KFB96_22630
HHC: M911_03930
TNI: TVNIR_2171(asrB_[H])
TTI: THITH_06470
APRS: BI364_04835
HSI: BOX17_10630
MGEO: CFI10_06210
ENM: EBS_0042
CHIZ: HQ393_09265
SLAC: SKTS_06280
GSK: KN400_0060(hdrF)
GME: Gmet_3431(hdrF)
GEM: GM21_0025
GEO: Geob_3718(hdrF)
GLO: Glov_0869
GBM: Gbem_0026(hdrF)
GBN: GEOBRER4_00240(hdrF)
DVL: Dvul_0831
DVM: DvMF_0327
DDS: Ddes_2103
DTR: RSDT_0570(flxA)
DFL: DFE_0760
DMA: DMR_01960
DGG: DGI_1054(floxA)
DPI: BN4_11864
DBA: Dbac_0854
DSF: UWK_01339
DAL: Dalk_5060
DAT: HRM2_22060(dsrB1)
DTO: TOL2_C24220(asrB1) TOL2_C28800(asrB2)
DOV: DSCO28_27850(hdrF_1) DSCO28_36110(hdrF_2)
DWD: DSCW_47570(hdrF_1) DSCW_60910(hdrF_2)
DALK: DSCA_54470(hdrF)
DMM: dnm_084940(pyrK1)
ADE: Adeh_0748
SAT: SYN_02220
SFU: Sfum_1970
DBR: Deba_2136
BLAG: BLTE_14890
RCH: RUM_11020
RUM: CK1_05100
BPRO: PMF13cell1_01676(asrB_1)
PTH: PTH_1405(UbiB)
DAU: Daud_0569
CTHM: CFE_1624
CHY: CHY_0934
ADG: Adeg_1329
ALUS: STSP2_01454(asrB)
FVA: FV113G1_17780(asrB)
BOA: Bovatus_04662(asrB)
BCEL: BcellWH2_01246(asrB)
APS: CFPG_169
CPC: Cpar_0945
CLI: Clim_1196
PVI: Cvib_0839
PLT: Plut_1113
PROC: Ptc2401_02007(asrB)
PHO: PH1291(PH1291)
PAB: PAB0639(hydG-2) PAB1785
TKO: TK2071
THS: TES1_0165
TEU: TEU_09735
TCQ: TIRI35C_0408(shyC) TIRI35C_0920(hydG)
HUT: Huta_2603
HTI: HTIA_2363
HDS: HSR122_2939(mcr1)
TNE: Tneu_1104
KCR: Kcr_0323
BARB: AOA66_1502(shyC_1)
PSYT: DSAG12_03222(shyC_2) DSAG12_03717(hydG)
 » show all
Reference
PMID:8389482
  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
Proc Natl Acad Sci U S A 90:5341-4 (1993)
DOI:10.1073/pnas.90.11.5341
  Sequence
[pfu:PF0892]
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
J Bacteriol 182:1864-71 (2000)
DOI:10.1128/JB.182.7.1864-1871.2000
  Sequence
[pfu:PF1330]
LinkDB

KEGG   ORTHOLOGY: K17996
Entry
K17996                      KO                                     
Symbol
hydB
Name
sulfhydrogenase subunit beta (sulfur reductase) [EC:1.12.98.4]
Pathway
map00920  Sulfur metabolism
map01120  Microbial metabolism in diverse environments
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09102 Energy metabolism
   00920 Sulfur metabolism
    K17996  hydB; sulfhydrogenase subunit beta (sulfur reductase)
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.12  Acting on hydrogen as donor
   1.12.98  With other, known, physiological acceptors
    1.12.98.4  sulfhydrogenase
     K17996  hydB; sulfhydrogenase subunit beta (sulfur reductase)
Other DBs
RN: R10390
Genes
VNA: PN96_21150
VEJ: VEJY3_20406
PGB: H744_1c0420
PSTU: UIB01_19760
GNI: GNIT_2861
PAEW: KIH87_09715
ALG: AQULUS_13060(asrA)
ASIP: AQUSIP_08250(asrA)
LPN: lpg2470
LPH: LPV_2795
LPO: LPO_2659
LPM: LP6_2500
LPF: lpl2390
LPP: lpp2535
LPC: LPC_2008
LPA: lpa_03599
LPE: lp12_2462
LLO: LLO_2448
LOK: Loa_02483
TMC: LMI_1436
NHL: Nhal_1540
TEE: Tel_04910
TNI: TVNIR_2172(asrA_[H])
SLIM: SCL_2127
SVA: SVA_2156
ENM: EBS_0043
SLAC: SKTS_06270(hdrE)
DEU: DBW_2716
DFL: DFE_3282
DMA: DMR_01950
DGG: DGI_1053(floxB)
DDE: Dde_3529
DPI: BN4_11863
DBA: Dbac_0853
DSF: UWK_01338
DTO: TOL2_C24210(asrA1) TOL2_C28790(asrA2)
DWD: DSCW_47560(hydB-2_1) DSCW_60920(hydB-2_2)
DALK: DSCA_35360 DSCA_54480(hydB-2)
SAT: SYN_02219
SFU: Sfum_1971
BLAG: BLTE_14900
MSC: BN69_0849
MAGQ: MGMAQ_3145
MGM: Mmc1_0881
AFR: AFE_0940(hoxF)
RCH: RUM_11010
RUM: CK1_05090
BPRO: PMF13cell1_01675(asrA_1)
DAE: Dtox_1356
DAU: Daud_0568
CTHM: CFE_1625
MTHO: MOTHE_c07600(asrA1)
MTHZ: MOTHA_c08540(asrA1)
LPIL: LIP_0585
GPA: GPA_23160
AEQ: AEQU_0876
LBO: LBWT_7440
MIN: Minf_2384(napF)
MKC: kam1_2088
LCRE: Pla8534_67830(asrA)
GPN: Pan110_37770(asrA)
KST: KSMBR1_3671(asrA)
ALUS: STSP2_01455(asrA)
FVA: FV113G1_17790(asrA)
BOA: Bovatus_04661(asrA)
BCEL: BcellWH2_01247(asrA)
BLQ: L21SP5_01263(asrA)
RMR: Rmar_2586
PVI: Cvib_0840
PLT: Plut_1112
PAA: Paes_1926
PROC: Ptc2401_02006(asrA)
CTS: Ctha_0347
KOL: Kole_0574
CABY: Cabys_3226
PHO: PH1290(PH1290)
PAB: PAB0638(hydB-2) PAB1784
TKO: TK2072
THS: TES1_0164
TEU: TEU_09740
TCQ: TIRI35C_0409(shyB) TIRI35C_0921(hydB)
MTP: Mthe_0912
MHI: Mhar_2065
HUT: Huta_2602
HTI: HTIA_2362
MELU: MTLP_10630
ABI: Aboo_0083
KCR: Kcr_0324
BARB: AOA66_1501(shyB)
LOKI: Lokiarch_42540(shyB)
PSYT: DSAG12_03718(shyB)
 » show all
Reference
PMID:8389482
  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
Proc Natl Acad Sci U S A 90:5341-4 (1993)
DOI:10.1073/pnas.90.11.5341
  Sequence
[pfu:PF0891]
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
J Bacteriol 182:1864-71 (2000)
DOI:10.1128/JB.182.7.1864-1871.2000
  Sequence
[pfu:PF1329]
LinkDB

KEGG   ORTHOLOGY: K17993
Entry
K17993                      KO                                     
Symbol
hydA
Name
sulfhydrogenase subunit alpha [EC:1.12.1.3 1.12.1.5]
Pathway
map00920  Sulfur metabolism
map01120  Microbial metabolism in diverse environments
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09102 Energy metabolism
   00920 Sulfur metabolism
    K17993  hydA; sulfhydrogenase subunit alpha
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.12  Acting on hydrogen as donor
   1.12.1  With NAD+ or NADP+ as acceptor
    1.12.1.3  hydrogen dehydrogenase (NADP+)
     K17993  hydA; sulfhydrogenase subunit alpha
    1.12.1.5  hydrogen dehydrogenase [NAD(P)+]
     K17993  hydA; sulfhydrogenase subunit alpha
Other DBs
RN: R10390
GO: 0050583
Genes
AVL: AvCA_04400(hoxH)
AVD: AvCA6_04400(hoxH)
ACX: Achr_4370(hoxH)
MSQ: BKP64_00960
MARA: D0851_07215
PAEW: KIH87_09730
MICC: AUP74_02543(hoxH)
MII: BTJ40_11460
MICT: FIU95_09940(hoxH)
MHYD: GTQ55_08915
ALG: AQULUS_13030(hoxH)
ASIP: AQUSIP_08280(hoxH)
LPN: lpg2467(hydA)
LPH: LPV_2792
LPO: LPO_2656
LPM: LP6_2497(hydA)
LPF: lpl2387
LPP: lpp2532
LPC: LPC_2011(hydA)
LPA: lpa_03596
LPE: lp12_2459
LLO: LLO_2451
LOK: Loa_02480
LJR: NCTC11533_01742(hoxH)
LCJ: NCTC11976_02962(hoxH_2)
LSS: NCTC12082_00643(hoxH)
TMC: LMI_1439
MMAI: sS8_1970
FPH: Fphi_0819
FPT: BZ13_1196
FPI: BF30_1034
FPM: LA56_1343
FPX: KU46_521
FPZ: LA55_2066
FPJ: LA02_421
FRC: KX01_345
NHL: Nhal_1537
TEE: Tel_04930
TGR: Tgr7_1138
TVR: TVD_13260
HBE: BEI_0367
OCE: GU3_11735
SLIM: SCL_2124
SVA: SVA_2159
ENM: EBS_0040
BBAG: E1O_11220
TBD: Tbd_1263
DFL: DFE_3279
DSF: UWK_01341
DALK: DSCA_35400
SCL: sce4575(hoxH)
SAT: SYN_02222
BID: Bind_0507
MSC: BN69_0845
MGRY: MSR1_09580(hoxH)
MAGQ: MGMAQ_3149
AFR: AFE_0937(hoxH)
LPIL: LIP_0582
MMAN: MMAN_14450
MMC: Mmcs_3416
MKM: Mkms_3479
MJL: Mjls_3427
MMI: MMAR_3497
MHAD: B586_16670
MSHG: MSG_02854
MSTO: MSTO_04530
MSAK: MSAS_49690
MBAI: MB901379_03108(hoxH)
MSEO: MSEO_00850
MPSE: MPSD_35740
MHEK: JMUB5695_01550(hoxH)
MBRD: MBRA_29200
MSHJ: MSHI_09610
MTHN: 4412656_03555(hoxH)
MAIC: MAIC_21360
MANY: MANY_17730
NSR: NS506_04373(hydA)
RER: RER_34040
REQ: REQ_15170
SHY: SHJG_8772
SMAL: SMALA_7420
STRM: M444_33595
SRW: TUE45_pSRc_0046(hoxH)
SLAU: SLA_6981
SALJ: SMD11_1044
SFK: KY5_7225
SGE: DWG14_00279(hoxH)
SRO: Sros_4826
NCX: Nocox_21175(hoxH)
TBI: Tbis_1858
ACE: Acel_1019
KAL: KALB_4157
SNA: Snas_3474
ELE: Elen_1256
AEQ: AEQU_0879
LBO: LBWT_7400
MIN: Minf_2391(frhA)
MKC: kam1_2096
LCRE: Pla8534_67860(hoxH)
FMR: Fuma_01323(hoxH)
GMR: GmarT_18750(hoxH)
GPN: Pan110_37740(hoxH)
MRI: Mal4_24330(hoxH)
KST: KSMBR1_3674(hoxH)
ALUS: STSP2_01452(hoxH)
RMR: Rmar_2590
MGOT: MgSA37_01987(hoxH)
CPC: Cpar_0317
CCH: Cag_0245
CLI: Clim_2097
PPH: Ppha_2499
PAA: Paes_1929
PROC: Ptc2401_02009(hoxH)
CTS: Ctha_0344
CABY: Cabys_3229
DTP: JZK55_04700(hydA)
NIO: NITINOP_0586(hydA)
PHO: PH1294(PH1294)
PAB: PAB0641(hydA-2) PAB1787
TKO: TK2069
THA: TAM4_99
THS: TES1_0167
TEU: TEU_09725
TCQ: TIRI35C_0406(shyA) TIRI35C_0918(hydA)
HUT: Huta_2605
HTI: HTIA_2365
HDS: HSR122_2937(frhA)
ABI: Aboo_0080
NCV: NCAV_0543
KCR: Kcr_0321
BARB: AOA66_1504(hydA)
 » show all
Reference
PMID:2538471
  Authors
Bryant FO, Adams MW
  Title
Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus.
  Journal
J Biol Chem 264:5070-9 (1989)
  Sequence
[pfu:PF0894]
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
J Bacteriol 182:1864-71 (2000)
DOI:10.1128/JB.182.7.1864-1871.2000
  Sequence
[pfu:PF1332]
LinkDB

KEGG   ORTHOLOGY: K17994
Entry
K17994                      KO                                     
Symbol
hydD
Name
sulfhydrogenase subunit delta [EC:1.12.1.3 1.12.1.5]
Pathway
map00920  Sulfur metabolism
map01120  Microbial metabolism in diverse environments
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09102 Energy metabolism
   00920 Sulfur metabolism
    K17994  hydD; sulfhydrogenase subunit delta
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.12  Acting on hydrogen as donor
   1.12.1  With NAD+ or NADP+ as acceptor
    1.12.1.3  hydrogen dehydrogenase (NADP+)
     K17994  hydD; sulfhydrogenase subunit delta
    1.12.1.5  hydrogen dehydrogenase [NAD(P)+]
     K17994  hydD; sulfhydrogenase subunit delta
Other DBs
RN: R10390
GO: 0050583
Genes
ACX: Achr_4360(hoxY)
MSQ: BKP64_00955
MARA: D0851_07220
PAEW: KIH87_09725
MICC: AUP74_02544(hoxY)
MII: BTJ40_11465
MICT: FIU95_09945(hoxY)
MHYD: GTQ55_08910
ALG: AQULUS_13040(hoxY)
ASIP: AQUSIP_08270(hoxY)
LPN: lpg2468
LPH: LPV_2793
LPO: LPO_2657
LPM: LP6_2498
LPF: lpl2388
LPP: lpp2533
LPC: LPC_2010
LPA: lpa_03597
LPE: lp12_2460
LLO: LLO_2450
LOK: Loa_02481
LJR: NCTC11533_01743(hoxY)
LCJ: NCTC11976_02959(hoxY)
LSS: NCTC12082_00642(hoxY)
TMC: LMI_1438
MMAI: sS8_1969
FPH: Fphi_0818
FPT: BZ13_1195
FPI: BF30_1033
FPM: LA56_1342
FPX: KU46_522
FPZ: LA55_2065
FPJ: LA02_420
FNA: OOM_1816
FRC: KX01_346
NHL: Nhal_1538
TEE: Tel_04925
TGR: Tgr7_1137
TNI: TVNIR_2170(vhuG_[H])
TVR: TVD_13255
HBE: BEI_0366
OCE: GU3_11740
SLIM: SCL_2125
SVA: SVA_2158
ENM: EBS_0041
BBAG: E1O_11230
DFL: DFE_3280
DSF: UWK_01340
DALK: DSCA_35390
SAT: SYN_02221
BID: Bind_0506
MSC: BN69_0846
MGRY: MSR1_09590(hoxY)
MAGQ: MGMAQ_3148
MGM: Mmc1_0883
AFR: AFE_0938(hoxY)
LPIL: LIP_0583
MMAN: MMAN_14460
MMC: Mmcs_3417
MKM: Mkms_3480
MJL: Mjls_3428
MMI: MMAR_3498
MHAD: B586_16665
MSHG: MSG_02855
MSTO: MSTO_04520
MSAK: MSAS_49680
MBAI: MB901379_03109(hoxY)
MSEO: MSEO_00840
MPSE: MPSD_35750
MSHJ: MSHI_09600
MTHN: 4412656_03554(hoxY)
MAIC: MAIC_21370
MANY: MANY_17740
NSR: NS506_04374(mvhG)
SHY: SHJG_8771
SMAL: SMALA_7421
STRM: M444_33590
SRW: TUE45_pSRc_0047(hoxY)
SALJ: SMD11_1043
SFK: KY5_7224
SGE: DWG14_00278(hoxY)
ACE: Acel_1018
KAL: KALB_4152
SNA: Snas_3473
ELE: Elen_1255
GPA: GPA_23180
AEQ: AEQU_0878
LBO: LBWT_7410
MIN: Minf_2390(frhG)
MKC: kam1_2094
LCRE: Pla8534_67850(hoxY)
AAGG: ETAA8_22830(hoxY)
FMR: Fuma_01324(hoxY)
GMR: GmarT_18740(hoxY)
GPN: Pan110_37750(hoxY)
MRI: Mal4_24340(hoxY)
KST: KSMBR1_3673(hoxY)
ALUS: STSP2_01453(hoxY)
MGOT: MgSA37_01986(hoxY)
CPC: Cpar_0318
CLI: Clim_2096
PPH: Ppha_2498
PAA: Paes_1928
PROC: Ptc2401_02008(hoxY)
CABY: Cabys_3228
NIO: NITINOP_0587(hydD)
PHO: PH1292(PH1292)
PAB: PAB0640(hydD-2) PAB1786
TKO: TK2070
THS: TES1_0166
TEU: TEU_09730
TCQ: TIRI35C_0407(shyD) TIRI35C_0919(hydD)
HUT: Huta_2604
ABI: Aboo_0081
NCV: NCAV_0544
KCR: Kcr_0322
BARB: AOA66_1503(shyD)
PSYT: DSAG12_03219(shyD)
 » show all
Reference
PMID:2538471
  Authors
Bryant FO, Adams MW
  Title
Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus.
  Journal
J Biol Chem 264:5070-9 (1989)
  Sequence
[pfu:PF0893]
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
J Bacteriol 182:1864-71 (2000)
DOI:10.1128/JB.182.7.1864-1871.2000
  Sequence
[pfu:PF1331]
LinkDB

KEGG   ENZYME: 1.12.98.4
Entry
EC 1.12.98.4                Enzyme                                 
Name
sulfhydrogenase;
sulfur reductase
Class
Oxidoreductases;
Acting on hydrogen as donor;
With other, known, physiological acceptors
Sysname
H2:polysulfide oxidoreductase
Reaction(IUBMB)
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1 [RN:R10390]
Reaction(KEGG)
R10390
Substrate
H2 [CPD:C00282];
(sulfide)n [CPD:C19692]
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
ec00920  Sulfur metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K17995  sulfhydrogenase subunit gamma (sulfur reductase)
K17996  sulfhydrogenase subunit beta (sulfur reductase)
Genes
VNAPN96_21150
VEJVEJY3_20406
PGBH744_1c0420
PSTUUIB01_19760
PLALFXN65_14060
GNIGNIT_2861
PAEWKIH87_09715
ALGAQULUS_13060(asrA)
ASIPAQUSIP_08250(asrA)
LPNlpg2470
LPHLPV_2795
LPOLPO_2659
LPULPE509_00591
LPMLP6_2500
LPFlpl2390
LPPlpp2535
LPCLPC_2008
LPAlpa_03599
LPElp12_2462
LLOLLO_2448
LOKLoa_02483
LSHCAB17_17505
LIBE4T55_10910
LGTE4T54_10390
LJRNCTC11533_01745
LCJNCTC11976_02957
LSSNCTC12082_00640
TMCLMI_1436
TLOJ9253_17495
TSBHMY34_12570
NHLNhal_1540
NWRE3U44_15695
TMBThimo_0256
TEETel_04910
THIMKFB96_22630 KFB96_22635
HHCM911_03930 M911_03935
EBSECTOBSL9_1960
TNITVNIR_2171(asrB_[H]) TVNIR_2172(asrA_[H])
TTITHITH_06465 THITH_06470
APRSBI364_04830 BI364_04835
TTCFOKN1_2280
HSIBOX17_10630 BOX17_10635
MGEOCFI10_06210 CFI10_06215
MSECLN244_04730
NCUF0U83_02265
SLIMSCL_2127
SVASVA_2156
REVHUE57_13170
ENMEBS_0042 EBS_0043
CHIZHQ393_09260 HQ393_09265
CFONHZU75_11935 HZU75_11940
NOKFAY22_03470
SLACSKTS_06270(hdrE) SKTS_06280
GSKKN400_0060(hdrF)
GMEGmet_3431(hdrF)
GEMGM21_0025
GEBGM18_0022 GM18_3243
GPIGPICK_06780 GPICK_15715
GAOA2G06_16015
GURGura_0145 Gura_3587
GEOGeob_3718(hdrF)
GLOGlov_0869
GBMGbem_0026(hdrF)
GBNGEOBRER4_00240(hdrF) GEOBRER4_17920
GERKP004_08755 KP004_19720
GSUBKP001_06405 KP001_16595
GNTKP003_08280 KP003_19710
PPDPpro_2788 Ppro_2797
DESDSOUD_2753
DEUDBW_2716
DVEDESUT3_12210
DVLDvul_0831
DVMDvMF_0327
DVGDeval_2220 Deval_2221
DDSDdes_2103
DFIAXF13_12680
DPGDESPIGER_1695
DEFCNY67_01565
DTRRSDT_0570(flxA)
DFLDFE_0760 DFE_3282
DSDGD606_00165 GD606_07830 GD606_07835 GD606_13020
DMADMR_01950 DMR_01960
DCBC3Y92_00580 C3Y92_00585
DGGDGI_1053(floxB) DGI_1054(floxA)
DDEDde_1213 Dde_3529 Dde_3530
DMSE8L03_07155 E8L03_12035
DSADesal_0596
DHYDESAM_21326 DESAM_21327
DAFDesaf_2136 Desaf_2877
DPIBN4_11863 BN4_11864
DEJAWY79_02145
PSELGM415_09650 GM415_09655
DSXGD604_00275 GD604_05905 GD604_05910
DBADbac_0853 Dbac_0854
DOAAXF15_11180 AXF15_11185
DRTDret_0192 Dret_0193 Dret_2311 Dret_2312
DSFUWK_01338 UWK_01339
DAKDaAHT2_2013
DEOCAY53_08875
DALDalk_5060
DATHRM2_22060(dsrB1)
DTOTOL2_C24210(asrA1) TOL2_C24220(asrB1) TOL2_C28790(asrA2) TOL2_C28800(asrB2)
DOVDSCO28_27850(hdrF_1) DSCO28_36110(hdrF_2)
DWDDSCW_47560(hydB-2_1) DSCW_47570(hdrF_1) DSCW_60910(hdrF_2) DSCW_60920(hydB-2_2)
DALKDSCA_35360 DSCA_54470(hdrF) DSCA_54480(hydB-2)
DMMdnm_084940(pyrK1) dnm_084960
ADEAdeh_0748
ACPA2cp1_0799
AFWAnae109_0786
ANKAnaeK_0795
LLUAKJ09_02920
SATSYN_02219 SYN_02220
DAODesac_1690
SFUSfum_1970 Sfum_1971
DAXFDQ92_05240 FDQ92_05245
DBRDeba_2136
BLAGBLTE_14890 BLTE_14900
MSCBN69_0849
MROSEHO51_04970
MAGQMGMAQ_3145
MGMMmc1_0881
AFRAFE_0940(hoxF)
AFELferr_1058
AFIAcife_1818
AFJAFERRID_21570
CEUA7L45_12250 A7L45_12255
CTHDCDO33_09935 CDO33_09940
RCHRUM_11010 RUM_11020
RUMCK1_05090 CK1_05100
SMANC12CBH8_20580 C12CBH8_20590
BYLA4V09_16695 A4V09_16700
BPROPMF13cell1_01675(asrA_1) PMF13cell1_01676(asrB_1)
BLABEYS05_14065 EYS05_14070
DORDesor_2817
DAIDesaci_2626 Desaci_2627
DMIDesmer_2225 Desmer_2226
DCADesca_0133 Desca_0134 Desca_0139 Desca_0140
PTHPTH_1405(UbiB)
DRMDred_0140 Dred_0141 Dred_0147 Dred_0148
DRUDesru_0209 Desru_0210 Desru_0216 Desru_0217
DFGB0537_01505 B0537_01510 B0537_01540 B0537_01545 B0537_08750 B0537_08755
DAEDtox_1281 Dtox_1356 Dtox_1357
DKUDesku_1430 Desku_1480 Desku_1481
DAUDaud_0568 Daud_0569
TFRBR63_02790 BR63_09655 BR63_09660
FWADCMF_24640 DCMF_24645
TJRTherJR_0671 TherJR_0672 TherJR_0941 TherJR_1949 TherJR_1950
DGIDesgi_2042 Desgi_2043
CMIUB1H56_01500 B1H56_01505
VPYHZI73_20450 HZI73_20455
CTHMCFE_1624 CFE_1625
CHYCHY_0934
MTHOMOTHE_c07600(asrA1)
MTHZMOTHA_c08540(asrA1)
ADGAdeg_1329
MASMahau_0898 Mahau_0899
LPILLIP_0585
SNQCP978_06435
STIRDDW44_00710
SGZC0216_13090
GPAGPA_23160
AEQAEQU_0876
AHATADCFC_14540
RTSCE91St31_13770
LBOLBWT_7440
CYNCyan7425_2664
ABATCFX1CAM_1230 CFX1CAM_1231
PSUBPelsub_P0989
CAPCLDAP_19230
MINMinf_2384(napF)
MKCkam1_2088
LCREPla8534_67830(asrA)
GPNPan110_37770(asrA)
KSTKSMBR1_3671(asrA)
ALUSSTSP2_01454(asrB) STSP2_01455(asrA)
VAIBU251_07800 BU251_07805
TSUTresu_1319 Tresu_1320
TBETrebr_2030 Trebr_2031
TRCDYE49_06660 DYE49_06665
TPERIWA51_04925
FVAFV113G1_17780(asrB) FV113G1_17790(asrA)
FULC4N20_13340 C4N20_13345
FMOC4N19_02830
IPOIlyop_2560
BOABovatus_04661(asrA) Bovatus_04662(asrB)
BCELBcellWH2_01246(asrB) BcellWH2_01247(asrA)
DYSG7050_05275 G7050_05280
APSCFPG_169
ALDGFH31_00890 GFH31_00895
BLQL21SP5_01263(asrA)
RMRRmar_2586
RMGRhom172_2602
CPCCpar_0320 Cpar_0945 Cpar_0946
CLZBIU88_04770 BIU88_10280 BIU88_10285
CCHCag_1032 Cag_1566
CPHCpha266_1256 Cpha266_2166
CPBCphamn1_2129
CLIClim_1196 Clim_1197 Clim_2094
PVICvib_0839 Cvib_0840
PLTPlut_1112 Plut_1113
PPHPpha_1303 Ppha_2496
PAAPaes_1926
PROCPtc2401_02006(asrA) Ptc2401_02007(asrB)
PRSB9H02_09665 B9H02_09670
PROSCHL67_10245 CHL67_10250
CTSCtha_0347
HTEHydth_0591
SAFSULAZ_0892
PMXPERMA_0694
KOLKole_0574
KPFIX53_06755
CABYCabys_3226
TYETHEYE_A1851
DTPJZK55_04730 JZK55_23580
NKFNkreftii_000245
LFILFML04_0325
LFPY981_01645
LEGABH19_01770
TIDThein_2072
NLIG3M70_06675
AVEArcve_2105 Arcve_2106
ASTAsulf_01819 Asulf_01820
PFUPF0891 PF0892 PF1329 PF1330
PFIPFC_03665 PFC_03670 PFC_05860 PFC_05865
PHOPH1290(PH1290) PH1291(PH1291)
PABPAB0638(hydB-2) PAB0639(hydG-2) PAB1784 PAB1785
PYNPNA2_1554 PNA2_1555 PNA2_1667 PNA2_1668
PYAPYCH_00020 PYCH_00030 PYCH_08390 PYCH_08400
PYSPy04_0890 Py04_0891 Py04_1131 Py04_1132
PYCTQ32_02775 TQ32_02780 TQ32_03125 TQ32_03130
TKOTK2071 TK2072
TONTON_0054 TON_0055 TON_0536 TON_0537
TSITSIB_0282 TSIB_0283 TSIB_1520 TSIB_1521
TBATERMP_00067 TERMP_00068 TERMP_00538 TERMP_00539
THEGQS_02460 GQS_02465 GQS_04975 GQS_04980
THATAM4_114 TAM4_307 TAM4_579 TAM4_858
THMCL1_0141 CL1_0142 CL1_0641 CL1_0642
TLTOCC_03052 OCC_03057 OCC_12226 OCC_12231
THSTES1_0164 TES1_0165
TNUBD01_0439 BD01_0440 BD01_2065 BD01_2066
TEUTEU_09735 TEU_09740
TGYX802_03235 X802_03240 X802_07570 X802_07575
THVADU37_CDS02150 ADU37_CDS02160 ADU37_CDS16300 ADU37_CDS16310
TCHCHITON_0947 CHITON_0948 CHITON_1017 CHITON_1018
TPEPA0127_05285 A0127_05290 A0127_07145 A0127_07150
TPIEA7C91_06195 A7C91_06200 A7C91_08735 A7C91_08740
TGGA3K92_08490 A3K92_08495
TCEA3L02_00955 A3L02_00960 A3L02_02375 A3L02_02380
TBSA3L01_00930 A3L01_00935 A3L01_03425 A3L01_03430
THHCDI07_00930 CDI07_00935 CDI07_03365 CDI07_03370
TSLA3L11_04685 A3L11_04690 A3L11_07385 A3L11_07390
TTDA3L14_02385 A3L14_02390 A3L14_05110 A3L14_05115
TPRFA3L09_05675 A3L09_05680 A3L09_05730 A3L09_05735
TRLA3L10_03140 A3L10_03145 A3L10_05625 A3L10_05630
TPAFA3L08_06490 A3L08_06495
THYA3L12_05470 A3L12_05475
TICFH039_02785 FH039_02790 FH039_05980 FH039_05985
TCQTIRI35C_0408(shyC) TIRI35C_0409(shyB) TIRI35C_0920(hydG) TIRI35C_0921(hydB)
THEMFPV09_03365 FPV09_03370 FPV09_06565 FPV09_06570
PPACPAP_01500 PAP_01505 PAP_03240 PAP_03245
MTPMthe_0912
MHIMhar_2065
HUTHuta_2602 Huta_2603
HTIHTIA_2362 HTIA_2363
HALAHrd1104_08665
HDSHSR122_2939(mcr1)
HDFAArcSl_2418 AArcSl_2419
MELUMTLP_10630
ABIAboo_0083
ACFAciM339_0968
TNETneu_1104
CSUCSUB_C1019
KCRKcr_0323 Kcr_0324
BARBAOA66_1501(shyB) AOA66_1502(shyC_1)
LOKILokiarch_42540(shyB)
PSYTDSAG12_03222(shyC_2) DSAG12_03717(hydG) DSAG12_03718(shyB)
 » show all
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
2  [PMID:8389482]
  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
Proc Natl Acad Sci U S A 90:5341-4 (1993)
DOI:10.1073/pnas.90.11.5341
  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
4  [PMID:10714990]
  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
J Bacteriol 182:1864-71 (2000)
DOI:10.1128/JB.182.7.1864-1871.2000
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.12.98.4
IUBMB Enzyme Nomenclature: 1.12.98.4
ExPASy - ENZYME nomenclature database: 1.12.98.4
BRENDA, the Enzyme Database: 1.12.98.4
LinkDB

KEGG   REACTION: R10390
Entry
R10390                      Reaction                               
Name
H2:polysulfide oxidoreductase
Definition
Hydrogen + Polysulfide(n) <=> Hydrogen sulfide + Polysulfide(n-1)
Equation
C00282 + C19692(n) <=> C00283 + C19692(n-1)
Reaction class
RC03155  C00283_C19692
Enzyme
Pathway
rn00920  Sulfur metabolism
rn01120  Microbial metabolism in diverse environments
Orthology
K17993  sulfhydrogenase subunit alpha [EC:1.12.1.3 1.12.1.5]
K17994  sulfhydrogenase subunit delta [EC:1.12.1.3 1.12.1.5]
K17995  sulfhydrogenase subunit gamma (sulfur reductase) [EC:1.12.98.4]
K17996  sulfhydrogenase subunit beta (sulfur reductase) [EC:1.12.98.4]
Other DBs
RHEA: 35594
LinkDB

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