We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments HdrABC is an enzyme complex that is found in most methanogens and catalyses the reduction of the CoB-CoM heterodisulfide back to CoB and CoM. HdrA contains a FAD cofactor that acts as the entry point for electrons, which are transferred via HdrC to the HdrB catalytic subunit. One form of the enzyme from Methanosarcina acetivorans (HdrA2B2C2) can also catalyse EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase. cf. EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
2
oxidized ferredoxin [iron-sulfur] cluster
+
+
=
2
reduced ferredoxin [iron-sulfur] cluster
+
+
2
Synonyms
CoB-S-S-CoM reductase, Coenzyme B-Coenzyme M heterodisulfide reductase,
hdrA1B1C1 ,
hdrA2B2C2 ,
HdrABC , HdrB, HdrB2, HdrB2C2, heterodisulfide reductase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CoB-S-S-CoM reductase
-
-
Coenzyme B-Coenzyme M heterodisulfide reductase
-
-
heterodisulfide reductase
-
-
HdrABC
-
-
-
-
HdrB
-
subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM = 2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CoB,CoM:ferredoxin oxidoreductase
HdrABC is an enzyme complex that is found in most methanogens and catalyses the reduction of the CoB-CoM heterodisulfide back to CoB and CoM. HdrA contains a FAD cofactor that acts as the entry point for electrons, which are transferred via HdrC to the HdrB catalytic subunit. One form of the enzyme from Methanosarcina acetivorans (HdrA2B2C2) can also catalyse EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase. cf. EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized methyl viologen + CoB + CoM
reduced methyl viologen + CoM-S-S-CoB + H+
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
r
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
?
oxidized methyl viologen + CoB + CoM
reduced methyl viologen + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized methyl viologen + CoB + CoM
reduced methyl viologen + CoM-S-S-CoB + H+
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
-
-
-
r
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
r
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
-
-
-
r
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
[4Fe-4S]-center
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zn2+
-
required
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.05
CoM-S-S-CoB
-
subunit HdrB2C2, at 21ưC, pH not specified in the publication
1.1
CoB
-
subunit HdrB2, at 21ưC, pH not specified in the publication
1.2
CoB
-
subunit HdrB2C2, at 21ưC, pH not specified in the publication
1.2
CoM
-
subunit HdrB2, at 21ưC, pH not specified in the publication
1.4
CoM
-
subunit HdrB2C2, at 21ưC, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
subunit HdrB
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
HDRB_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
300
0
33068
Swiss-Prot
-
HDRC1_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
247
0
27921
Swiss-Prot
-
HDRC2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
161
0
18150
Swiss-Prot
-
HDRC_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
161
0
18120
Swiss-Prot
-
HDRA1_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
801
0
86966
Swiss-Prot
-
HDRA2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
793
0
86918
Swiss-Prot
-
HDRA_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
793
0
86803
Swiss-Prot
-
HDRB1_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
314
0
35327
Swiss-Prot
-
HDRB2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
300
0
32819
Swiss-Prot
-
A0A7G9Y787_9EURY
213
0
23444
TrEMBL
-
A0A7G9YVM5_9EURY
63
0
7033
TrEMBL
-
A0A7G9Y6Z0_9EURY
44
0
4900
TrEMBL
-
A0A7G9YR62_9EURY
300
0
32792
TrEMBL
-
HDRB_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
302
0
33458
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 18000, subunit HdrC2, SDS-PAGE
?
-
x * 33000, subunit HdrB2, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phenyl-Sepharose column chromatography, and Superdex 200 gel filtration
Q-Sepharose column chromatography and Superdex 200 gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3)-pCodonPlus-RIL cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
enzyme expression is upregulated in tetrathionate-grown cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ramos, A.R.; Grein, F.; Oliveira, G.P.; Venceslau, S.S.; Keller, K.L.; Wall, J.D.; Pereira, I.A.
The FlxABCD-HdrABC proteins correspond to a novel NADH dehydrogenase/heterodisulfide reductase widespread in anaerobic bacteria and involved in ethanol metabolism in Desulfovibrio vulgaris Hildenborough
Environ. Microbiol.
17
2288-2305
2015
Desulfovibrio vulgaris, Desulfovibrio vulgaris ATCC 29579
brenda
Kroeninger, L.; Berger, S.; Welte, C.; Deppenmeier, U.
Evidence for the involvement of two heterodisulfide reductases in the energy-conserving system of Methanomassiliicoccus luminyensis
FEBS J.
283
472-483
2016
Methanomassiliicoccus luminyensis, Methanomassiliicoccus luminyensis DSM 25720
brenda
Yan, Z.; Wang, M.; Ferry, J.G.
A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide reductase with homologs in the domains Bacteria and Archaea
mBio
8
e02285-16
2017
Methanosarcina acetivorans
brenda
Hamann, N.; Mander, G.J.; Shokes, J.E.; Scott, R.A.; Bennati, M.; Hedderich, R.
A cysteine-rich CCG domain contains a novel [4Fe-4S] cluster binding motif as deduced from studies with subunit B of heterodisulfide reductase from Methanothermobacter marburgensis
Biochemistry
46
12875-12885
2007
Methanothermobacter marburgensis (Q50755)
brenda
Mangold, S.; Valdes, J.; Holmes, D.S.; Dopson, M.
Sulfur metabolism in the extreme acidophile Acidithiobacillus caldus
Front. Microbiol.
10
17
2011
Acidithiobacillus caldus
brenda
Fielding, A.J.; Parey, K.; Ermler, U.; Scheller, S.; Jaun, B.; Bennati, M.
Advanced electron paramagnetic resonance on the catalytic iron-sulfur cluster bound to the CCG domain of heterodisulfide reductase and succinate quinone reductase
J. Biol. Inorg. Chem.
18
905-915
2013
Methanothermobacter marburgensis
brenda
Buan, N.R.; Metcalf, W.W.
Methanogenesis by Methanosarcina acetivorans involves two structurally and functionally distinct classes of heterodisulfide reductase
Mol. Microbiol.
75
843-853
2010
Methanosarcina acetivorans
brenda
Select items on the left to see more content.
html completed