[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-18; 210-226; 425-435; 455-459 AND 641-650. 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]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 651-659. PubMed=8617278 [NCBI, ExPASy, EBI, Israel, Japan] Vaupel M., Dietz H., Linder D., Thauer R.K.; "Primary structure of cyclohydrolase (Mch) from Methanobacterium thermoautotrophicum (strain Marburg) and functional expression of the mch gene in Escherichia coli."; Eur. J. Biochem. 236:294-300(1996).
[3]	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).
[4]	ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE, AND PROTEIN SEQUENCE OF 2-18. 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).
[5]	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). May act as the catalytic subunit.
CATALYTIC ACTIVITY: Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O³-phospho-L-threonine + dihydromethanophenazine.
COFACTOR: Binds 4 4Fe-4S clusters per subunit.
COFACTOR: FAD.
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 hdrA family.
SIMILARITY: Contains 4 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

X81134; CAA57039.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X92083; CAA63065.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S48720; S48720.

3D structure databases

HSSP

P07485; 1DWL. [HSSP ENTRY / PDB]

ModBase

Q50756.

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).
QuickGo view.

Family and domain databases

InterPro

IPR001450; 4Fe4S_Fe_S_bd.
IPR006076; FAD-dep_OxRdtase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Pfam

PF01266; DAO; 1.
PF00037; Fer4; 4.
PF00070; Pyr_redox; 1.
Pfam graphical view of domain structure.

PRINTS

PR00353; 4FE4SFRDOXIN.
PR00411; PNDRDTASEI.

PROSITE

PS00198; 4FE4S_FER_1; 4.
PS51379; 4FE4S_FER_2; 4.
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; FAD; Flavoprotein; 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`	`2 659`	`658`	`CoB--CoM heterodisulfide reductase iron-sulfur subunit A.`	`PRO_0000150062`
`DOMAIN`	`244 274`	`31`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`292 321`	`30`	`4Fe-4S ferredoxin-type 2.`
`DOMAIN`	`581 610`	`30`	`4Fe-4S ferredoxin-type 3.`
`DOMAIN`	`611 640`	`30`	`4Fe-4S ferredoxin-type 4.`
`NP_BIND`	`158 181`	`24`	`FAD (Potential).`
`METAL`	`254 254`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`257 257`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`260 260`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`264 264`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`301 301`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`304 304`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`307 307`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`311 311`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`591 591`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`METAL`	`594 594`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`METAL`	`597 597`		`Iron-sulfur 3 (4Fe-4S) (Potential).`
`METAL`	`601 601`		`Iron-sulfur 4 (4Fe-4S) (Potential).`
`METAL`	`620 620`		`Iron-sulfur 4 (4Fe-4S) (Potential).`
`METAL`	`623 623`		`Iron-sulfur 4 (4Fe-4S) (Potential).`
`METAL`	`626 626`		`Iron-sulfur 4 (4Fe-4S) (Potential).`
`METAL`	`630 630`		`Iron-sulfur 3 (4Fe-4S) (Potential).`

Sequence information

Length: 659 AA [This is the length of the unprocessed precursor]

Molecular weight: 72182 Da [This is the MW of the unprocessed precursor]

CRC64: FC01196FEE3A5F9E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEEKKETME EPKIGVYVCH CGVNIGGVVD VEAVRDYAAK LPNVVIAKDY KYYCSDPGQL 

        70         80         90        100        110        120 
EIQKDIKELG INRVVVAACS PRLHEPTFRR CVEEAGLNQF LFEFANIREH DSWVHMDNPE 

       130        140        150        160        170        180 
GATEKAKDLV RMAVAKARLL EPLEASKVSV DDKALVIGGG VAGIQAALDL ADMGFKTYMV 

       190        200        210        220        230        240 
EKRPSISGRM GQLDKTFPTL DCSMCILAPK MVDVGKHDNI ELITYAEVKE VDGYIGNFKV 

       250        260        270        280        290        300 
KIEKKPRYID EELCTGCGSC VEVCPIEMPN YFDEGIGMTK AVYIPFPQAV PLCATIDKDY 

       310        320        330        340        350        360 
CIECMLCDEV CERGAVKHDQ EPEEIEIEVG TIIVATGYDA YDPTEKLEYG YGRHTNVITG 

       370        380        390        400        410        420 
LELERMINAS GPTDGKVLKP SDGEKPKRVA FIHCVGSRDE QIGKPYCSRV CCMYIMKNAQ 

       430        440        450        460        470        480 
LIKDKMPDTE VTLYYMDIRA FGKGFEEFYK RSQEKYGIKF IRGRPAEVIE NPDLTLTVRS 

       490        500        510        520        530        540 
EDTLLGKVTE YDYDMVVLGV GLVPPEGAET LRQTIGLSKS ADGFLMEAHP KLRPVDTLTD 

       550        560        570        580        590        600 
GVYLAGVAQG PKDIPDAVAQ ASGAAARAAI PMVKGEVEIE PIIAVTDSDV CGGCEVCIEL 

       610        620        630        640        650 
CPFGAISIEE GHANVNVALC KGCGTCVAAC PSGAMDQQHF KTEQIMAQIE AALNEPASK

Q50756 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