[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=9063468 [NCBI, ExPASy, EBI, Israel, Japan] Kuenkel A., Vaupel M., Heim S., Thauer R.K., Hedderich R.; "Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme."; Eur. J. Biochem. 244:226-234(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1128/JB.00810-06; PubMed=16980466 [NCBI, ExPASy, EBI, Israel, Japan] Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.; "The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."; J. Bacteriol. 188:7922-7931(2006).
[3]	PROTEIN SEQUENCE OF 2-20, FUNCTION, AND SUBUNIT. PubMed=8174566 [NCBI, ExPASy, EBI, Israel, Japan] Heiden S., Hedderich R., Setzke E., Thauer R.K.; "Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri."; Eur. J. Biochem. 221:855-861(1994).

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). HdrD 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 2 4Fe-4S clusters per subunit.
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 two subunits; hdrD and hdrE.
SIMILARITY: Belongs to the hdrD 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

Y09870; CAA70997.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000099; AAZ70545.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S43468; S43468.

RefSeq

YP_305125.1; -.

3D structure databases

ModBase

P96797.

Enzyme and pathway databases

BioCyc

MBAR269797:MBAR_A1599-MON; -.

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.
IPR004017; Cys_rich_region.
IPR012285; Fum_reductase_C.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.1060.10; Fum_reductase_C; 1.

Pfam

PF02754; CCG; 2.
PF00037; Fer4; 1.
Pfam graphical view of domain structure.

PRINTS

PR00353; 4FE4SFRDOXIN.

PROSITE

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

BLOCKS

P96797.

Genome annotation databases

GeneID

3624318; -.

GenomeReviews

CP000099_GR; Mbar_A1599.

KEGG

mba:Mbar_A1599; -.

NMPDR

fig|269797.3.peg.1907; -.

Phylogenomic databases

HOGENOM

P96797; -.

Genome annotation databases

CMR

P96797; Mbar_A1599.

Other

ProtoNet

P96797.

UniRef

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

Keywords

4Fe-4S; Complete proteome; 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`	`2 409`	`408`	`CoB--CoM heterodisulfide reductase iron-sulfur subunit D.`	`PRO_0000150080`
`DOMAIN`	`14 44`	`31`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`81 110`	`30`	`4Fe-4S ferredoxin-type 2.`
`METAL`	`24 24`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`27 27`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`30 30`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`METAL`	`34 34`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`90 90`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`93 93`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`96 96`		`Iron-sulfur 2 (4Fe-4S) (Potential).`
`METAL`	`100 100`		`Iron-sulfur 1 (4Fe-4S) (Potential).`
`CONFLICT`	`43 44`		`KP -> HQ (in Ref. 1; CAA70997).`

Sequence information

Length: 409 AA [This is the length of the unprocessed precursor]

Molecular weight: 45055 Da [This is the MW of the unprocessed precursor]

CRC64: 1AC01503AA1F5BDE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKRTPSIDT KNLTAVQLME LDACVRCGEC VKWCPTYAAS GGKPGLAPRD KILRWRQYMN 

        70         80         90        100        110        120 
KSYGLKAKLF GPQEVSPSEL EEFKDDVHGC TTCGVCATVC EAGINTVEIW EAIRTNLVKK 

       130        140        150        160        170        180 
GIGPYGKQSA FPKLVGQYHN PYMKDQKDRL AWVPPDVKIE DKADIVYFTG CTAGYNQLAL 

       190        200        210        220        230        240 
AFATSRVLNK LGIKFAMLGE EEWCCGSALI RTGQVHVDDV ARELARHNVE ALQKKGAKKV 

       250        260        270        280        290        300 
LFACAGCFRA AKIDWPRLLG KELPFEVIHI TQFLADLIQA DKIKWEKPIN KTITYHDPCH 

       310        320        330        340        350        360 
LGRHVGVFNA PRYVLSHIPG VKFVEMDRSK EFQRCCGAGG GVKAGMPDLA VAMGESRVKD 

       370        380        390        400 
ALETNADILS SACPFCKRNL SDGRDALKSD IVVEDIIELV AEALGLSTS

P96797 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