CoB--CoM heterodisulfide reductase iron-sulfur subunit A - Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133)

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Reviewed, UniProtKB/Swiss-Prot Q50756 (HDRA_METTM)

Last modified May 5, 2009. Version 61. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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

Gene names

Name:

hdrA

Organism

Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133)

Taxonomic identifier

79929 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

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Protein attributes

Sequence length	659 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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). May act as the catalytic subunit. Ref.3
Catalytic activity	Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + dihydromethanophenazine.
Cofactor	Binds 4 4Fe-4S clusters per subunit. Ref.3 FAD. Ref.3
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.3
Sequence similarities	Belongs to the hdrA family. Contains 4 4Fe-4S ferredoxin-type domains.

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Ontologies

Keywords
Biological process	Methanogenesis
Domain	Repeat
Ligand	4Fe-4S FAD Flavoprotein Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	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 tRNA processing Inferred from electronic annotation. Source: InterPro
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 FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1 Ref.4

Chain

2 – 659

658

CoB--CoM heterodisulfide reductase iron-sulfur subunit A

PRO_0000150062

Regions

Domain

244 – 274

4Fe-4S ferredoxin-type 1

Domain

292 – 321

4Fe-4S ferredoxin-type 2

Domain

581 – 610

4Fe-4S ferredoxin-type 3

Domain

611 – 640

4Fe-4S ferredoxin-type 4

Nucleotide binding

158 – 181

FAD Potential

Sites

Metal binding

254

Iron-sulfur 1 (4Fe-4S) Potential Ref.1

Metal binding

257

Iron-sulfur 1 (4Fe-4S) Potential Ref.1

Metal binding

260

Iron-sulfur 1 (4Fe-4S) Potential Ref.1

Metal binding

264

Iron-sulfur 2 (4Fe-4S) Potential Ref.1

Metal binding

301

Iron-sulfur 2 (4Fe-4S) Potential Ref.1

Metal binding

304

Iron-sulfur 2 (4Fe-4S) Potential Ref.1

Metal binding

307

Iron-sulfur 2 (4Fe-4S) Potential Ref.1

Metal binding

311

Iron-sulfur 1 (4Fe-4S) Potential Ref.1

Metal binding

591

Iron-sulfur 3 (4Fe-4S) Potential Ref.1

Metal binding

594

Iron-sulfur 3 (4Fe-4S) Potential Ref.1

Metal binding

597

Iron-sulfur 3 (4Fe-4S) Potential Ref.1

Metal binding

601

Iron-sulfur 4 (4Fe-4S) Potential Ref.1

Metal binding

620

Iron-sulfur 4 (4Fe-4S) Potential Ref.1

Metal binding

623

Iron-sulfur 4 (4Fe-4S) Potential Ref.1

Metal binding

626

Iron-sulfur 4 (4Fe-4S) Potential Ref.1

Metal binding

630

Iron-sulfur 3 (4Fe-4S) Potential Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q50756-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FC01196FEE3A5F9E
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FASTA

659

72,182

        10         20         30         40         50         60 
MAEEKKETME EPKIGVYVCH CGVNIGGVVD VEAVRDYAAK LPNVVIAKDY KYYCSDPGQL 

        70         80         90        100        110        120 
EIQKDIKELG INRVVVAACS PRLHEPTFRR CVEEAGLNQF LFEFANIREH DSWVHMDNPE 

       130        140        150        160        170        180 
GATEKAKDLV RMAVAKARLL EPLEASKVSV DDKALVIGGG VAGIQAALDL ADMGFKTYMV 

       190        200        210        220        230        240 
EKRPSISGRM GQLDKTFPTL DCSMCILAPK MVDVGKHDNI ELITYAEVKE VDGYIGNFKV 

       250        260        270        280        290        300 
KIEKKPRYID EELCTGCGSC VEVCPIEMPN YFDEGIGMTK AVYIPFPQAV PLCATIDKDY 

       310        320        330        340        350        360 
CIECMLCDEV CERGAVKHDQ EPEEIEIEVG TIIVATGYDA YDPTEKLEYG YGRHTNVITG 

       370        380        390        400        410        420 
LELERMINAS GPTDGKVLKP SDGEKPKRVA FIHCVGSRDE QIGKPYCSRV CCMYIMKNAQ 

       430        440        450        460        470        480 
LIKDKMPDTE VTLYYMDIRA FGKGFEEFYK RSQEKYGIKF IRGRPAEVIE NPDLTLTVRS 

       490        500        510        520        530        540 
EDTLLGKVTE YDYDMVVLGV GLVPPEGAET LRQTIGLSKS ADGFLMEAHP KLRPVDTLTD 

       550        560        570        580        590        600 
GVYLAGVAQG PKDIPDAVAQ ASGAAARAAI PMVKGEVEIE PIIAVTDSDV CGGCEVCIEL 

       610        620        630        640        650 
CPFGAISIEE GHANVNVALC KGCGTCVAAC PSGAMDQQHF KTEQIMAQIE AALNEPASK

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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 2-18; 210-226; 425-435; 455-459 AND 641-650.
[2]	"Primary structure of cyclohydrolase (Mch) from Methanobacterium thermoautotrophicum (strain Marburg) and functional expression of the mch gene in Escherichia coli." Vaupel M., Dietz H., Linder D., Thauer R.K. Eur. J. Biochem. 236:294-300(1996) [PubMed: 8617278] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 651-659.
[3]	"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.
[4]	"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 2-18.
[5]	"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.

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Cross-references

Sequence databases
	X81134 Genomic DNA. Translation: CAA57039.1. X92083 Genomic DNA. Translation: CAA63065.1.
PIR	S48720.
3D structure databases
HSSP	HSSP built from PDB template 1DWL based on UniProtKB P07485.
ModBase	Search...
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR001450. 4Fe4S_Fe_S_bd_subgr. IPR017900. 4Fe4S_Fe_S_CS. IPR002218. GIDA-rel. [Graphical view]
Pfam	PF00037. Fer4. 4 hits. PF01134. GIDA. 1 hit. [Graphical view]
PROSITE	PS00198. 4FE4S_FER_1. 4 hits. PS51379. 4FE4S_FER_2. 4 hits. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

HDRA_METTM

Accession

Primary (citable) accession number: Q50756
Secondary accession number(s): Q50752

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 23, 2007
Last modified:	May 5, 2009
This is version 61 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Family and domain databases

Entry information

Relevant documents