Reviewed, UniProtKB/Swiss-Prot Q8TIB9 (HDRC_METAC)

Names and origin

Protein names

Recommended name:
    CoB--CoM heterodisulfide reductase 1 iron-sulfur subunit C
    EC=1.8.98.1

Gene names

Name:	hdrC
Ordered Locus Names:	MA_4236

Organism

Methanosarcina acetivorans [Complete proteome] [HAMAP]

Taxonomic identifier

2214 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
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) By similarity.
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 M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide: step 1/1.
Subunit structure	The heterodisulfide reductase 1 is composed of three subunits; hdrA, hdrB and hdrC By similarity.
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	Complete proteome
Gene Ontology (GO)
Biological process	cofactor metabolic process Inferred from electronic annotation. Source: InterPro 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 – 161	161	CoB--CoM heterodisulfide reductase 1 iron-sulfur subunit C		PRO_0000150072
Regions
	Domain	10 – 40	31	4Fe-4S ferredoxin-type 1
	Domain	51 – 82	32	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	19	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	22	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	25	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	29	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	62	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	65	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	68	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	72	1	Iron-sulfur 1 (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8TIB9-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 3D0339845B0DD95C	FASTA	161	18,150
	10 20 30 40 50 60 MSEELLKLLK AEGLDLLSCM HCGICTGSCP SGRHTGLNTR RIIRDARKNR AAVLSDYDLW 70 80 90 100 110 120 LCTTCYTCQE RCPRGIPITD AILELRRLAV REGLMLPEHR FVSEMVLECG HAVPLDEETK 130 140 150 160 KKREELGLDP IPETVQKDPE ALEGLKTLLK TCKFDELVAK K

References

[1]

"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity." Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P. , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B. Genome Res. 12:532-542(2002) [PubMed: 11932238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE010299 Genomic DNA. Translation: AAM07581.1.
RefSeq	NP_619101.1.
3D structure databases
SMR	Q8TIB9. Positions 15-97.
ModBase	Search...
Genome annotation databases
GeneID	1476130.
GenomeReviews	Gene locus MA_4236 in contig AE010299_GR.
KEGG	mac:MA4236.
NMPDR	fig|188937.1.peg.4127.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG542047.
OMA	HTGLNTR.
Enzyme and pathway databases
BioCyc	MACE188937:MA4236-MONOMER.
BRENDA	1.8.98.1. 275708.
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. IPR009051. Helical_ferredxn. [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_METAC

Accession

Primary (citable) accession number: Q8TIB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2002
Last modified:	February 9, 2010
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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