Reviewed, UniProtKB/Swiss-Prot Q50754 (HDRC_METTM)

Names and origin

Protein names

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

Gene names

Name:

hdrC

Organism

Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133)

Taxonomic identifier

79929 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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). HdrC may carry electrons from hydrogenase to hdrA. 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 Probable.
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 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. Ref.2
Sequence similarities	Belongs to the hdrC 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	Direct protein sequencing
Gene Ontology (GO)
Biological process	cofactor metabolic process Inferred from electronic annotation. Source: InterPro methanogenesis Ref.2 Inferred from direct assay. Source: UniProtKB oxidation reduction Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW CoB--CoM heterodisulfide reductase activity Ref.2 Inferred from direct assay. Source: UniProtKB 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
	Initiator methionine	1	1	Removed Ref.1 Ref.3
	Chain	2 – 185	184	CoB--CoM heterodisulfide reductase iron-sulfur subunit C		PRO_0000150078
Regions
	Domain	25 – 55	31	4Fe-4S ferredoxin-type 1
	Domain	68 – 99	32	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	35	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	38	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	41	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	45	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	79	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	82	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	85	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	89	1	Iron-sulfur 1 (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q50754-1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 757BA97AC5488086	FASTA	185	20,610
	10 20 30 40 50 60 MTLLQREENI IRKGNIDKEF SEKIKAAGGD SLEYCFQCGT CTGSCPSGRR TPYRVRQIIR 70 80 90 100 110 120 KANVGLKDEI ISDPTLWMCT TCYYCQERCP RKVKIVDVVK LARNEAAKAG FMAPAHKALG 130 140 150 160 170 180 SFVIKTGHGV PINDATMELR KAVGLGELPP TTHQFPEALE EVQKIIKATG FDQLIGYNWE TGELE

References

[1]	"The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine-nucleotide-dependent thioredoxin reductases." Hedderich R., Koch J., Linder D., Thauer R.K. Eur. J. Biochem. 225:253-261(1994) [PubMed: 7925445] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-25.
[2]	"Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)." Hedderich R., Berkessel A., Thauer R.K. Eur. J. Biochem. 193:255-261(1990) [PubMed: 2121478] [Abstract] Cited for: FUNCTION, COFACTOR, SUBUNIT.
[3]	"H2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties." Setzke E., Hedderich R., Heiden S., Thauer R.K. Eur. J. Biochem. 220:139-148(1994) [PubMed: 8119281] [Abstract] Cited for: ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE, PROTEIN SEQUENCE OF 2-25.
[4]	"Physiological role of the F420-non-reducing hydrogenase (Mvh) from Methanothermobacter marburgensis." Stojanowic A., Mander G.J., Duin E.C., Hedderich R. Arch. Microbiol. 180:194-203(2003) [PubMed: 12856108] [Abstract] Cited for: ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X81133 Genomic DNA. Translation: CAA57037.1.
PIR	S78508.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR017680. CoB/CoM_hetero-S_Rdtase_csu. IPR012285. Fum_reductase_C. [Graphical view]
Gene3D	G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
TIGRFAMs	TIGR03290. CoB_CoM_SS_C. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HDRC_METTM

Accession

Primary (citable) accession number: Q50754

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 56 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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