Entry
Name
dihydromethanophenazine:CoB-CoM heterodisulfide reductase;
hdrDE (gene names);
CoB---CoM heterodisulfide reductase (ambiguous);
heterodisulfide reductase (ambiguous);
coenzyme B:coenzyme M:methanophenazine oxidoreductase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With other, known, physiological acceptors
BRITE hierarchy
Sysname
CoB:CoM:methanophenazine oxidoreductase
Reaction(IUBMB)
CoB + CoM + methanophenazine = CoM-S-S-CoB + dihydromethanophenazine [RN:
R04540 ]
Reaction(KEGG)
Substrate
Product
CoM-S-S-CoB [CPD:
C04832 ];
dihydromethanophenazine [CPD:
C11904 ]
Comment
This enzyme, found in methanogenic archaea that belong to the Methanosarcinales order, regenerates CoM and CoB after the action of EC
2.8.4.1 , coenzyme-B sulfoethylthiotransferase. It is a membrane-bound enzyme that contains (per heterodimeric unit) two distinct b-type hemes and two [4Fe-4S] clusters. cf. EC
1.8.7.3 , ferredoxin:CoB-CoM heterodisulfide reductase, EC
1.8.98.5 , H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC
1.8.98.6 , formate:CoB-CoM heterodisulfide,ferredoxin reductase and EC
1.8.98.4 , coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase.
History
EC 1.8.98.1 created 2003, modified 2017
Pathway
ec01120 Microbial metabolism in diverse environments
Orthology
K08264 heterodisulfide reductase subunit D
K08265 heterodisulfide reductase subunit E
Genes
DTO : TOL2_C11570 TOL2_C26590
DTI : Desti_0745 Desti_5348 Desti_5359
DMP : FAK_08500 FAK_17480 FAK_17510 FAK_21900 FAK_22170
CBAM : PIECOFPK_02827(fadF_2)
SDJ : NCTC13534_04277(glpC)
STHA : NCTC11429_03180(glpC)
PHG : KCTC32516_00052(fadF_1)
KAN : IMCC3317_06930(lutA)
SPON : HME9304_02805(glcD)
CJG : NCTC13459_02299(glpC)
BFD : NCTC4823_02385(fadF_3)
DBC : MFMK1_003223 MFMK1_003224
SSID : SPSIL_030490(fadF_1)
SACV : SPACI_036000(fadF_2)
SBAE : DSM104329_00833(fadF_2)
MBA : Mbar_A1598 Mbar_A1599
MBY : MSBRM_2859 MSBRM_2860
MBW : MSBRW_3132 MSBRW_3133
MBAR : MSBR2_2817 MSBR2_2818
MBAK : MSBR3_1887 MSBR3_1888
MAC : MA_0687(hdrE) MA_0688(hdrD)
MMA : MM_1843(hdrE) MM_1844(hdrD)
MMAZ : MmTuc01_1919 MmTuc01_1920
MMJ : MSMAS_2838 MSMAS_2839
MMAC : MSMAC_1591 MSMAC_1592
MVC : MSVAZ_2770 MSVAZ_2771
MEK : MSKOL_2763 MSKOL_2764
MLS : MSLAZ_0424 MSLAZ_0425
METM : MSMTP_2735 MSMTP_2736
MEF : MSWH1_0437 MSWH1_0438
MEQ : MSWHS_0448 MSWHS_0449
MSJ : MSSAC_0623 MSSAC_0624
MSZ : MSSIH_0574 MSSIH_0575
MSW : MSSIT_0606 MSSIT_0607
MTHR : MSTHT_2243 MSTHT_2244
MTHE : MSTHC_1036 MSTHC_1037
MHOR : MSHOH_3536 MSHOH_3537
MFZ : AOB57_004610 AOB57_004615
MBU : Mbur_0470 Mbur_2436 Mbur_2437
MMET : MCMEM_0578 MCMEM_0579 MCMEM_0900
MELO : J7W08_00925 J7W08_00930 J7W08_03275
MMH : Mmah_0146 Mmah_0632 Mmah_0633 Mmah_0921
MHAZ : BHR79_00205 BHR79_00210 BHR79_02695 BHR79_08975
MPOT : BKM01_08205 BKM01_08210 BKM01_08800
MEV : Metev_0541 Metev_0542 Metev_1534
MZH : Mzhil_0597 Mzhil_0598
MZI : HWN40_03860 HWN40_03865 HWN40_05290
MMAV : RE476_04650 RE476_06370 RE476_06375
MSEB : RE474_00905 RE474_02145 RE474_02150
MHZ : Metho_1043 Metho_1505 Metho_1506
MEHF : MmiHf6_06590(fadF_1) MmiHf6_06600
MEES : MmiEs2_03520 MmiEs2_03530(fadF_1)
MCJ : MCON_3441(hdrE) MCON_3442(hdrD)
MEAE : QEN48_02165 QEN48_02170
BARC : AOA65_0539(hdrD_2) AOA65_0555(hdrD_3) AOA65_1721(hdrD_4) AOA65_2237(hdrD_5)
BARB : AOA66_1745(hdrD_3) AOA66_1757(hdrD_4)
LOKI : Lokiarch_00520(hdrD_1) Lokiarch_07600(hdrD_4) Lokiarch_10620(hdrD_5) Lokiarch_19710(hdrD_6) Lokiarch_23220 Lokiarch_23520(hdrD_7) Lokiarch_26320(hdrD_9) Lokiarch_40880(hdrD_11)
LOB : NEF87_004080 NEF87_004857
PSYT : DSAG12_01123 DSAG12_02413 DSAG12_02953
» show all
Taxonomy
Reference
Authors
Hedderich R, Berkessel A, Thauer RK
Title
Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg).
Journal
Reference
Authors
Abken HJ, Tietze M, Brodersen J, Baumer S, Beifuss U, Deppenmeier U.
Title
Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Go1.
Journal
Reference
Authors
Simianu M, Murakami E, Brewer JM, Ragsdale SW.
Title
Purification and properties of the heme- and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila.
Journal
Reference
Authors
Murakami E, Deppenmeier U, Ragsdale SW.
Title
Characterization of the intramolecular electron transfer pathway from 2-hydroxyphenazine to the heterodisulfide reductase from Methanosarcina thermophila.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 1.8.98.1
ExPASy - ENZYME nomenclature database: 1.8.98.1