Reviewed, UniProtKB/Swiss-Prot P96797 (HDRD_METBF)

Names and origin

Protein names

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

Gene names

Name:	hdrD
Ordered Locus Names:	Mbar_A1599

Organism

Methanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]

Taxonomic identifier

269797 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	409 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). HdrD may act as the catalytic subunit.
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.
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 two subunits; hdrD and hdrE.
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 Direct protein sequencing
Gene Ontology (GO)
Biological process	methanogenesis Ref.3 Inferred from direct assay. Source: UniProtKB 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 Ref.3 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
	Chain	2 – 409	408	CoB--CoM heterodisulfide reductase iron-sulfur subunit D		PRO_0000150080
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
Experimental info
	Sequence conflict	43 – 44	2	KP → HQ in CAA70997. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P96797-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 1AC01503AA1F5BDE	FASTA	409	45,055
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme." Kuenkel A., Vaupel M., Heim S., Thauer R.K., Hedderich R. Eur. J. Biochem. 244:226-234(1997) [PubMed: 9063468] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes." 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. J. Bacteriol. 188:7922-7931(2006) [PubMed: 16980466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri." Heiden S., Hedderich R., Setzke E., Thauer R.K. Eur. J. Biochem. 221:855-861(1994) [PubMed: 8174566] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20, FUNCTION, SUBUNIT.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y09870 Genomic DNA. Translation: CAA70997.1. CP000099 Genomic DNA. Translation: AAZ70545.1.
PIR	S43468.
RefSeq	YP_305125.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3624318.
GenomeReviews	Gene locus Mbar_A1599 in contig CP000099_GR.
KEGG	mba:Mbar_A1599.
NMPDR	fig|269797.3.peg.1907.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P96797.
Enzyme and pathway databases
BioCyc	MBAR269797:MBAR_A1599-MON.
Family and domain databases
InterPro	IPR001450. 4Fe4S_Fe_S_bd. 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. PF00037. Fer4. 1 hit. [Graphical view]
PRINTS	PR00353. 4FE4SFRDOXIN.
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HDRD_METBF

Accession

Primary (citable) accession number: P96797
Secondary accession number(s): Q46C47, Q9UWK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 66 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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