[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-25. PubMed=7925445 [NCBI, ExPASy, EBI, Israel, Japan] Hedderich R., Koch J., Linder D., Thauer R.K.; "The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine-nucleotide-dependent thioredoxin reductases."; Eur. J. Biochem. 225:253-261(1994).
[2]	FUNCTION, COFACTOR, AND SUBUNIT. PubMed=2121478 [NCBI, ExPASy, EBI, Israel, Japan] Hedderich R., Berkessel A., Thauer R.K.; "Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)."; Eur. J. Biochem. 193:255-261(1990).
[3]	ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE, AND PROTEIN SEQUENCE OF 2-25. PubMed=8119281 [NCBI, ExPASy, EBI, Israel, Japan] Setzke E., Hedderich R., Heiden S., Thauer R.K.; "H2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties."; Eur. J. Biochem. 220:139-148(1994).
[4]	ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE. DOI=10.1007/s00203-003-0577-9; PubMed=12856108 [NCBI, ExPASy, EBI, Israel, Japan] Stojanowic A., Mander G.J., Duin E.C., Hedderich R.; "Physiological role of the F420-non-reducing hydrogenase (Mvh) from Methanothermobacter marburgensis."; Arch. Microbiol. 180:194-203(2003).

Comments

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). HdrC may carry electrons from hydrogenase to hdrA.
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 (Probable).
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. It forms a complex with the F420-non-reducing hydrogenase (Mvh), which provides the reducing equivalents to the heterodisulfide reductase.
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

X81133; CAA57037.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S78508; S78508.

3D structure databases

ModBase

Q50754.

Ontologies

GO:0051912;	Molecular function: CoB--CoM heterodisulfide reductase activity (inferred from direct assay from UniProtKB).
GO:0015948;	Biological process: methanogenesis (inferred from direct assay from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (non-traceable author statement from UniProtKB).
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.

PROSITE

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

Other

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

Keywords

4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Oxidoreductase; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 185`	`184`	`CoB--CoM heterodisulfide reductase iron-sulfur subunit C.`	`PRO_0000150078`
`DOMAIN`	`25 55`	`31`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`68 99`	`32`	`4Fe-4S ferredoxin-type 2.`
`METAL`	`35 35`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`38 38`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`41 41`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`45 45`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`79 79`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`82 82`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`85 85`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`89 89`		`Iron-sulfur 1 (4Fe-4S) (Potential).`

Sequence information

Length: 185 AA [This is the length of the unprocessed precursor]

Molecular weight: 20610 Da [This is the MW of the unprocessed precursor]

CRC64: 757BA97AC5488086 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTLLQREENI IRKGNIDKEF SEKIKAAGGD SLEYCFQCGT CTGSCPSGRR TPYRVRQIIR 

        70         80         90        100        110        120 
KANVGLKDEI ISDPTLWMCT TCYYCQERCP RKVKIVDVVK LARNEAAKAG FMAPAHKALG 

       130        140        150        160        170        180 
SFVIKTGHGV PINDATMELR KAVGLGELPP TTHQFPEALE EVQKIIKATG FDQLIGYNWE 


TGELE

Q50754 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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