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).

[2]

FUNCTION, AND SOURCE OF ELECTRONS.
STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
DOI=10.1016/S0014-5793(98)00555-9; PubMed=9654152 [NCBI, ExPASy, EBI, Israel, Japan]
Baeumer S., Murakami E., Brodersen J., Gottschalk G., Ragsdale S.W., Deppenmeier U.;
"The F420H2:heterodisulfide oxidoreductase system from Methanosarcina species. 2-Hydroxyphenazine mediates electron transfer from F420H2 dehydrogenase to heterodisulfide reductase.";
FEBS Lett. 428:295-298(1998).

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 (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 2 is composed of two subunits; hdrD and hdrE (By similarity).
MISCELLANEOUS: Methanophenazine seems to mediate electron transfer from a F420-non-reducing hydrogenase to the heterodisulfide reductase 2.
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

AE008384; AAM31540.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_633868.1; -.

3D structure databases

ModBase

Q8PVW3.

Enzyme and pathway databases

BioCyc

MMAZ192952:MM1844-MON; -.

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

Q8PVW3.

Genome annotation databases

GeneID

1480186; -.

GenomeReviews

AE008384_GR; MM_1844.

KEGG

mma:MM_1844; -.

NMPDR

fig|192952.1.peg.1844; -.

Phylogenomic databases

HOGENOM

Q8PVW3; -.

Genome annotation databases

CMR

Q8PVW3; MM_1844.

Other

ProtoNet

Q8PVW3.

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`	`1 409`	`409`	`CoB--CoM heterodisulfide reductase 2 iron-sulfur subunit D.`	`PRO_0000150081`
`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).`

Sequence information

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

Molecular weight: 45377 Da [This is the MW of the unprocessed precursor]

CRC64: F74FA592197FAC46 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKKTPSIDT KNLTAVQLME LDSCTRCGEC VKWCPTYAAS GQKPGLAPRD KILRWRQFMN 

        70         80         90        100        110        120 
KSYGIKAKLF GPTEIPQSEL EEFKDDVHGC TTCGICATVC ESGINTVELW EALRTNLVKK 

       130        140        150        160        170        180 
GIGPFGKQNM FPKLIGQYHN PYMKDQKDRL NWVPPDVKIE DKADVVYFTG CTAGYNQLAL 

       190        200        210        220        230        240 
AFATARVLNK LGVKFSMLGE EEWCCGSALI RTGQVHVDDV PRELARHNVE ALKKKGAKKV 

       250        260        270        280        290        300 
LYACAGCFRA SKVDWPRLLG EELPFEVVHV AEFLADLIKQ DKIKWEKSIN KTVTYHDPCH 

       310        320        330        340        350        360 
LGRHVGVFDA PRYVLSHIPG VKFVEMDRVK EFQRCCGAGG GVKAGIPDLA LGVAESRVKD 

       370        380        390        400 
AVATDADILS SCCPFCKRNL MDGRDSLKVD MVVEDVIELV AEALGLETK

Q8PVW3 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