Reviewed,
UniProtKB/Swiss-Prot O27434 (HDRA_METTH)
Last modified
November 25, 2008.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
| ||||
| Organism | Methanobacterium thermoautotrophicum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 187420 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter |
Protein attributes
| Sequence length | 659 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). May act as the catalytic subunit By similarity. |
| 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 By similarity. FAD By similarity. |
| Pathway | |
| 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 By similarity. |
| Sequence similarities | Belongs to the hdrA family. Contains 4 4Fe-4S ferredoxin-type domains. |
Ontologies
Keywords | |
|---|---|
| Biological process | Methanogenesis |
| Domain | Repeat |
| Ligand | 4Fe-4S FAD Flavoprotein 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 reductionInferred 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 activityInferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred 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 – 659 | 659 | CoB--CoM heterodisulfide reductase iron-sulfur subunit A | PRO_0000150061 | |||||
Regions | |||||||||
| Domain | 245 – 275 | 31 | 4Fe-4S ferredoxin-type 1 | ||||||
| Domain | 293 – 322 | 30 | 4Fe-4S ferredoxin-type 2 | ||||||
| Domain | 582 – 611 | 30 | 4Fe-4S ferredoxin-type 3 | ||||||
| Domain | 612 – 641 | 30 | 4Fe-4S ferredoxin-type 4 | ||||||
| Nucleotide binding | 159 – 182 | 24 | FAD Potential | ||||||
Sites | |||||||||
| Metal binding | 255 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
| Metal binding | 258 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
| Metal binding | 261 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
| Metal binding | 265 | 1 | Iron-sulfur 2 (4Fe-4S) Potential | ||||||
| Metal binding | 302 | 1 | Iron-sulfur 2 (4Fe-4S) Potential | ||||||
| Metal binding | 305 | 1 | Iron-sulfur 2 (4Fe-4S) Potential | ||||||
| Metal binding | 308 | 1 | Iron-sulfur 2 (4Fe-4S) Potential | ||||||
| Metal binding | 312 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
| Metal binding | 592 | 1 | Iron-sulfur 3 (4Fe-4S) Potential | ||||||
| Metal binding | 595 | 1 | Iron-sulfur 3 (4Fe-4S) Potential | ||||||
| Metal binding | 598 | 1 | Iron-sulfur 3 (4Fe-4S) Potential | ||||||
| Metal binding | 602 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 621 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 624 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 627 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 631 | 1 | Iron-sulfur 3 (4Fe-4S) Potential | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. Reeve J.N.J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H. |
Cross-references
Sequence databases | |
|---|---|
| AE000666 Genomic DNA. Translation: AAB85858.1. Different initiation. | |
| PIR | G69050. |
| RefSeq | NP_276497.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DWL based on UniProtKB P07485. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1471098. |
| GenomeReviews | Gene locus MTH_1381 in contig AE000666_GR. |
| KEGG | mth:MTH1381. |
| NMPDR | fig|187420.1.peg.1352. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O27434. |
Enzyme and pathway databases | |
| BioCyc | MTHE187420:MTH1381-MON. |
Family and domain databases | |
| InterPro | IPR001450. 4Fe4S_Fe_S_bd. IPR006076. FAD-dep_OxRdtase. IPR001100. Pyr_nuc-diS_OxRdtase. [Graphical view] |
| Pfam | PF01266. DAO. 1 hit. PF00037. Fer4. 4 hits. [Graphical view] |
| PRINTS | PR00353. 4FE4SFRDOXIN. PR00411. PNDRDTASEI. |
| PROSITE | PS00198. 4FE4S_FER_1. 4 hits. PS51379. 4FE4S_FER_2. 4 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| LinkHub | O27434. |
Entry information
| Entry name | HDRA_METTH | ||||||||
| Accession | Primary (citable) accession number: O27434 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


