Reviewed, UniProtKB/Swiss-Prot Q8PVW3 (HDRD_METMA)

Names and origin

Protein names

Recommended name:
    CoB--CoM heterodisulfide reductase 2 iron-sulfur subunit D
    EC=1.8.98.1

Gene names

Name:	hdrD
Ordered Locus Names:	MM_1844

Organism

Methanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP]

Taxonomic identifier

2209 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. Ref.2
Catalytic activity	Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-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 structure	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.
Sequence similarities	Belongs to the hdrD family. Contains 2 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Biological process	Methanogenesis
Domain	Repeat
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW CoB--CoM heterodisulfide reductase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 409	409	CoB--CoM heterodisulfide reductase 2 iron-sulfur subunit D		PRO_0000150081
Regions
	Domain	14 – 44	31	4Fe-4S ferredoxin-type 1
	Domain	81 – 110	30	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	24	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	27	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	30	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	34	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	90	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	93	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	96	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	100	1	Iron-sulfur 1 (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8PVW3-1 [UniParc]. Last modified January 16, 2004. Version 2. Checksum: F74FA592197FAC46	FASTA	409	45,377
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." 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. J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.
[2]	"The F420H2:heterodisulfide oxidoreductase system from Methanosarcina species. 2-Hydroxyphenazine mediates electron transfer from F420H2 dehydrogenase to heterodisulfide reductase." Baeumer S., Murakami E., Brodersen J., Gottschalk G., Ragsdale S.W., Deppenmeier U. FEBS Lett. 428:295-298(1998) [PubMed: 9654152] [Abstract] Cited for: FUNCTION, SOURCE OF ELECTRONS. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008384 Genomic DNA. Translation: AAM31540.1. Different initiation.
RefSeq	NP_633868.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1480186.
GenomeReviews	Gene locus MM_1844 in contig AE008384_GR.
KEGG	mma:MM_1844.
NMPDR	fig|192952.1.peg.1844.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8PVW3.
Enzyme and pathway databases
BioCyc	MMAZ192952:MM1844-MON.
BRENDA	1.8.98.1. 261165.
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR004017. Cys_rich_region. IPR012285. Fum_reductase_C. [Graphical view]
Gene3D	G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
Pfam	PF02754. CCG. 2 hits. [Graphical view]
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HDRD_METMA

Accession

Primary (citable) accession number: Q8PVW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 16, 2004
Last modified:	March 24, 2009
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)