KEGG   ENZYME: 1.8.2.3
Entry
EC 1.8.2.3                  Enzyme                                 

Name
sulfide-cytochrome-c reductase (flavocytochrome c)
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With a cytochrome as acceptor
Sysname
hydrogen-sulfide:flavocytochrome c oxidoreductase
Reaction(IUBMB)
hydrogen sulfide + 2 ferricytochrome c = sulfur + 2 ferrocytochrome c + 2 H+ [RN:R09499]
Reaction(KEGG)
R09499
Substrate
hydrogen sulfide [CPD:C00283];
ferricytochrome c [CPD:C00125]
Product
sulfur [CPD:C00087];
ferrocytochrome c [CPD:C00126];
H+ [CPD:C00080]
Comment
The enzyme from Allochromatium vinosum contains covalently bound FAD and covalently-bound c-type hemes.
History
EC 1.8.2.3 created 2011
Pathway
ec00920  Sulfur metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K17229  sulfide dehydrogenase [flavocytochrome c] flavoprotein chain
Genes
PFUW: KF707C_21980
PCZ: PCL1606_32160
PSEM: TO66_14415
PSET: THL1_2615
PKE: DLD99_13450
MLQ: ASQ50_12760
MCA: MCA1800
METU: GNH96_09675
MMT: Metme_2643
MDN: JT25_000975
METL: U737_15565
MMAI: sS8_1791
HMAR: HVMH_0551(fccB-2)
MEJ: Q7A_2824
MEC: Q7C_1163
TSE: THMIRHAS_18290(fccB-2_1) THMIRHAS_20620(fccB-2_2) THMIRHAS_20630(fccB-2_3) THMIRHAS_20660(fccB-2_4) THMIRHAS_22910
TZO: THMIRHAT_07270(fccB-2_1) THMIRHAT_11110(fccB-2_2) THMIRHAT_19250(fccB-2_3)
TIG: THII_1691
THIP: N838_11065
AEH: Mlg_1674
HHK: HH1059_07180(fccB-2)
TKM: TK90_0236
TVR: TVD_01535
HCO: LOKO_02303(fccB)
AJP: AMJAP_1601(fccB)
SLIM: SCL_0077
TBN: TBH_C2099
RSC: RCFBP_10218(soxF)
RSL: RPSI07_0185(soxF)
RSN: RSPO_c00202(soxF)
RSM: CMR15_10205(soxF)
RSE: F504_3303
RSY: RSUY_02370(fccB)
RPI: Rpic_3460
RIN: ACS15_3558(fccB)
CNC: CNE_1c35250(fccB)
RME: Rmet_3426(soxF)
CTI: RALTA_A3028(soxF)
CGD: CR3_2737
BTD: BTI_5302(fccB)
BUL: BW21_4949(fccB)
PNU: Pnuc_0728
PPNO: DA70_17165
PPNM: LV28_13585
PPUL: RO07_07525
PSPU: NA29_03405
PAPI: SG18_07965
LMIR: NCTC12852_01642(fccB_1)
AMIM: MIM_c36690
AFQ: AFA_06230
POL: Bpro_4437
PNA: Pnap_1666
CTES: O987_23255
RTA: Rta_13730
LIM: L103DPR2_01211(fccB)
LIH: L63ED372_00495(fccB)
HYB: Q5W_03625
HPSE: HPF_06250(fccB)
CBAA: SRAA_1125
CBAB: SMCB_0868(soxF)
LCH: Lcho_3772
THI: THI_2406 THI_3462(fccB)
RGE: RGE_20240(soxF) RGE_28930
SHD: SUTH_01079(soxF)
MEH: M301_0792
MEP: MPQ_0937(hcaD)
MBAC: BN1209_0603(fccB)
SDR: SCD_n00382(soxF)
SPLB: SFPGR_23320(dhsU)
URU: DSM104443_01345(fccB)
UPL: DSM104440_01253(fccB)
DSU: Dsui_1540
OTR: OTERR_06870(soxF)
AZO: azo1141(soxF)
AOA: dqs_1252
AZA: AZKH_1225(soxF)
BPRC: D521_0589
SULR: B649_04290
ATP: ATR_0804
ACIB: ACBT_1002
ACRE: ACRYA_0730
APOC: APORC_1120
AELL: AELL_1865
AAQI: AAQM_1701
ASUI: ASUIS_0989
ACLO: ACLO_1688
ALK: ALEK_1722
AMYT: AMYT_0522
AMAR: AMRN_0551
ACAA: ACAN_0575
AMOL: AMOL_0465
HBV: ABIV_2582
PACO: AACT_1978
ARC: ABLL_1981
SUN: SUN_0058
NIS: NIS_0032
SMX: SM11_pC0584(soxF)
SMI: BN406_04790(soxF)
SMER: DU99_20770
SFH: SFHH103_05249(soxF)
SFD: USDA257_c56690(fccB)
BRA: BRADO2412
BRS: S23_52640
AOL: S58_51890
BRAD: BF49_1953
BARH: WN72_15005
BVZ: BRAD3257_5957(fccB)
VGO: GJW-30_1_03540(fccB)
BOS: BSY19_756
XAU: Xaut_1514
MET: M446_3049
MNO: Mnod_4566
MAQU: Maq22A_c24650(hcaD)
HDN: Hden_1401
HMC: HYPMC_2198(fccB)
FIL: BN1229_v1_2541(fccB) BN1229_v1_3674(fccB)
FIY: BN1229_v1_3376(fccB) BN1229_v1_3668(fccB)
MCG: GL4_0655
BVR: BVIR_2065
BLAG: BLTE_06870(fccB-2_1) BLTE_06880 BLTE_08550(fccB-2_2)
PLEO: OHA_1_01453(hcaD1)
HDI: HDIA_1477(fccB)
RBM: TEF_09470
PSF: PSE_1359(soxF)
SIL: SPO1001(soxF)
RUT: FIU92_04335(fccB)
RCP: RCAP_rcc03294(fccB)
RLI: RLO149_c031800(soxF)
DSH: Dshi_2799(fccB)
OTM: OSB_13270(fccB)
PTP: RCA23_c03060(soxF1)
MALG: MALG_03478
RSU: NHU_02672(soxF)
RMM: ROSMUCSMR3_02021(fccB)
RID: RIdsm_01806(fccB)
ROH: FIU89_03910(fccB)
LVS: LOKVESSMR4R_03402(fccB)
AHT: ANTHELSMS3_02241(fccB)
MARU: FIU81_10265(fccB)
ROT: FIV09_13390(fccB1)
MALU: KU6B_10840(fccB-2)
HNE: HNE_2480
SHUM: STHU_33030
MAG: amb2173
MGY: MGMSRv2__0553(fccB) MGMSRv2__1259(fccB)
MGRY: MSR1_09980(fccB_1) MSR1_16630(fccB_2)
MAGX: XM1_2729(fccB) XM1_2927(fccB)
MAGQ: MGMAQ_1800(fccB) MGMAQ_1840(fccB) MGMAQ_1853(soxF)
MGM: Mmc1_2996
HTL: HPTL_0808(soxF)
CTE: CT1015(fccB-1) CT2081(fccB-2)
CLI: Clim_0011
PAA: Paes_0011
PROC: Ptc2401_00011(fccB_1) Ptc2401_00848(fccB_2)
CTS: Ctha_0643
 » show all
Reference
1  [PMID:4357558]
  Authors
Kusai K, Yamanaka T
  Title
The oxidation mechanisms of thiosulphate and sulphide in Chlorobium thiosulphatophilum: roles of cytochrome c-551 and cytochrome c-553.
  Journal
Biochim Biophys Acta 325:304-14 (1973)
DOI:10.1016/0005-2728(73)90106-0
Reference
2  [PMID:222744]
  Authors
Fukumori Y, Yamanaka T
  Title
Flavocytochrome c of Chromatium vinosum. Some enzymatic properties and subunit structure.
  Journal
J Biochem 85:1405-14 (1979)
DOI:10.1093/oxfordjournals.jbchem.a132467
  Sequence
Reference
3  [PMID:6301383]
  Authors
Gray GO, Gaul DF, Knaff DB
  Title
Partial purification and characterization of two soluble c-type cytochromes from  Chromatium vinosum.
  Journal
Arch Biochem Biophys 222:78-86 (1983)
DOI:10.1016/0003-9861(83)90504-0
Reference
4  [PMID:7939681]
  Authors
Chen ZW, Koh M, Van Driessche G, Van Beeumen JJ, Bartsch RG, Meyer TE, Cusanovich MA, Mathews FS
  Title
The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium.
  Journal
Science 266:430-2 (1994)
DOI:10.1126/science.7939681
  Sequence
Reference
5  [PMID:9613590]
  Authors
Sorokin DYu, de Jong GA, Robertson LA, Kuenen GJ
  Title
Purification and characterization of sulfide dehydrogenase from alkaliphilic chemolithoautotrophic sulfur-oxidizing bacteria.
  Journal
FEBS Lett 427:11-4 (1998)
DOI:10.1016/S0014-5793(98)00379-2
Reference
6  [PMID:10809687]
  Authors
Kostanjevecki V, Brige A, Meyer TE, Cusanovich MA, Guisez Y, van Beeumen J
  Title
A membrane-bound flavocytochrome c-sulfide dehydrogenase from the purple phototrophic sulfur bacterium Ectothiorhodospira vacuolata.
  Journal
J Bacteriol 182:3097-103 (2000)
DOI:10.1128/JB.182.11.3097-3103.2000
Other DBs
ExplorEnz - The Enzyme Database: 1.8.2.3
IUBMB Enzyme Nomenclature: 1.8.2.3
ExPASy - ENZYME nomenclature database: 1.8.2.3
BRENDA, the Enzyme Database: 1.8.2.3

DBGET integrated database retrieval system