FUNCTION: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B) (By similarity).
CATALYTIC ACTIVITY: Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O³-phospho-L-threonine + dihydromethanophenazine.
COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity).
PATHWAY: Cofactor metabolism; coenzyme B/coenzyme M regeneration; coenzyme B and coenzyme M from CoB-CoM heterodisulfide: step 1/1 .
SUBUNIT: The heterodisulfide reductase is composed of three subunits; hdrA, hdrB and hdrC (By similarity).
SIMILARITY: Belongs to the hdrC family.
SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE010351; AAM01788.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_613858.1; -.

3D structure databases

ModBase

Q8TXT7.

Enzyme and pathway databases

BioCyc

MKAN190192:MK0573-MON; -.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051912;	Molecular function: CoB--CoM heterodisulfide reductase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0015948;	Biological process: methanogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001450; 4Fe4S_Fe_S_bd.
IPR017680; CoB/CoM_hetero-S_rdtase_csu.
IPR012285; Fum_reductase_C.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.1060.10; Fum_reductase_C; 1.

PRINTS

PR00353; 4FE4SFRDOXIN.

PROSITE

PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8TXT7.

Genome annotation databases

1476674; -.

AE009439_GR; MK0573.

mka:MK0573; -.

fig|190192.1.peg.571; -.

Phylogenomic databases

HOGENOM

Q8TXT7; -.

Genome annotation databases

CMR

Q8TXT7; MK0573.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Oxidoreductase; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 192`	`192`	`CoB--CoM heterodisulfide reductase iron-sulfur subunit C.`	`PRO_0000150075`
`DOMAIN`	`32 61`	`30`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`75 105`	`31`	`4Fe-4S ferredoxin-type 2.`
`METAL`	`41 41`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`44 44`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`47 47`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`51 51`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`85 85`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`88 88`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`91 91`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`95 95`		`Iron-sulfur 1 (4Fe-4S) (Potential).`

Sequence information

Length: 192 AA [This is the length of the unprocessed precursor]

Molecular weight: 22022 Da [This is the MW of the unprocessed precursor]

CRC64: 2645D1648F85F4DB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVEPRDTVIR EEDLNPDFLE ELSELVEPVF EEEEVLSVQA CYQCGTCTGS CPSGRRTSYR 

        70         80         90        100        110        120 
TRLIMRKLQL GLVDEVIKSD ELWMCTTCYT CYERCPRGVK IVDAVKAARN LAAKKGYMAK 

       130        140        150        160        170        180 
AHRMVAMFVI KTGHAVPIND EIREVRKNIG LDEVPPTTHR YEEALEEVQK LVKINEFDKL 

       190 
IGYDWEEGDL VD

Q8TXT7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools