NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
PubMed=12125824 [NCBI, ExPASy, EBI, Israel, Japan]
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.;
"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.";
J. Mol. Microbiol. Biotechnol. 4:453-461(2002).

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) (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 1 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

AE008384; AAM30675.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_633003.1; -.

3D structure databases

ModBase

Q8PY84.

Enzyme and pathway databases

BioCyc

MMAZ192952:MM0979-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

Q8PY84.

Genome annotation databases

GeneID

1479321; -.

GenomeReviews

AE008384_GR; MM_0979.

KEGG

mma:MM_0979; -.

NMPDR

fig|192952.1.peg.979; -.

Phylogenomic databases

HOGENOM

Q8PY84; -.

Genome annotation databases

CMR

Q8PY84; MM_0979.

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`	`1 161`	`161`	`CoB--CoM heterodisulfide reductase 1 iron-sulfur subunit C.`	`PRO_0000150076`
`DOMAIN`	`10 40`	`31`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`51 82`	`32`	`4Fe-4S ferredoxin-type 2.`
`METAL`	`19 19`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`22 22`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`25 25`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`29 29`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`62 62`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`65 65`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`68 68`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`72 72`		`Iron-sulfur 1 (4Fe-4S) (Potential).`

Sequence information

Length: 161 AA [This is the length of the unprocessed precursor]

Molecular weight: 18120 Da [This is the MW of the unprocessed precursor]

CRC64: 40F05C2B90FC23BA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEELLKVLK AAGLDVLSCM HCGTCTGSCP SGRHTGLNTR RIIRDARKNR ATVLSDDALW 

        70         80         90        100        110        120 
LCTTCYTCQE RCPRGIPITD ALLELRRLAV RKGFMRPEHR RVSELVLECG HAVPLDEETK 

       130        140        150        160 
KKREELGLDP IPETVQKYPE ALEELKALLK TCKFDELAAE K

Q8PY84 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