Reviewed,
UniProtKB/Swiss-Prot Q6LWL2 (HDRA_METMP)
Last modified
November 25, 2008.
Version 43.
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 | Methanococcus maripaludis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 39152 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus |
Protein attributes
| Sequence length | 658 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 1 is composed of three subunits; hdrA, hdrB and hdrC By similarity. |
| Sequence similarities | Belongs to the hdrA family. Contains 4 4Fe-4S ferredoxin-type domains. |
Ontologies
Keywords | |
|---|---|
| Biological process | Methanogenesis |
| Coding sequence diversity | Selenocysteine |
| Domain | Repeat |
| Ligand | 4Fe-4S FAD Flavoprotein Iron Iron-sulfur Metal-binding Selenium |
| 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 FAD bindingInferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW selenium 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 – 658 | 658 | CoB--CoM heterodisulfide reductase iron-sulfur subunit A | PRO_0000318646 | |||||
Regions | |||||||||
| Domain | 236 – 267 | 32 | 4Fe-4S ferredoxin-type 1 | ||||||
| Domain | 284 – 313 | 30 | 4Fe-4S ferredoxin-type 2 | ||||||
| Domain | 575 – 604 | 30 | 4Fe-4S ferredoxin-type 3 | ||||||
| Domain | 607 – 637 | 31 | 4Fe-4S ferredoxin-type 4 | ||||||
| Nucleotide binding | 150 – 173 | 24 | FAD Potential | ||||||
Sites | |||||||||
| Metal binding | 246 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
| Metal binding | 249 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
| Metal binding | 252 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
| Metal binding | 256 | 1 | Iron-sulfur 2 (4Fe-4S) Potential | ||||||
| Metal binding | 293 | 1 | Iron-sulfur 2 (4Fe-4S) Potential | ||||||
| Metal binding | 296 | 1 | Iron-sulfur 2 (4Fe-4S) Potential | ||||||
| Metal binding | 299 | 1 | Iron-sulfur 2 (4Fe-4S) Potential | ||||||
| Metal binding | 303 | 1 | Iron-sulfur 1 (4Fe-4S) Potential | ||||||
| Metal binding | 584 | 1 | Iron-sulfur 3 (4Fe-4S) Potential | ||||||
| Metal binding | 587 | 1 | Iron-sulfur 3 (4Fe-4S) Potential | ||||||
| Metal binding | 590 | 1 | Iron-sulfur 3 (4Fe-4S) Potential | ||||||
| Metal binding | 594 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 617 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 620 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 623 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 627 | 1 | Iron-sulfur 3 (4Fe-4S) Potential | ||||||
Amino acid modifications | |||||||||
| Non-standard residue | 197 | 1 | Selenocysteine Probable | ||||||
Sequences
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References
| [1] | "Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis." Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., Moore B.C. Leigh J.A.J. Bacteriol. 186:6956-6969(2004) [PubMed: 15466049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S2 / LL. |
Cross-references
Sequence databases | |
|---|---|
| BX950229 Genomic DNA. Translation: CAF31253.1. | |
| RefSeq | NP_988817.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BD6 based on UniProtKB Q45560. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2762636. |
| GenomeReviews | Gene locus MMP1697 in contig BX950229_GR. |
| KEGG | mmp:MMP1697. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q6LWL2. |
Family and domain databases | |
| InterPro | IPR001450. 4Fe4S_Fe_S_bd. IPR006076. FAD-dep_OxRdtase. IPR016040. NAD(P)-bd. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF01266. DAO. 1 hit. PF00037. Fer4. 4 hits. PF00070. Pyr_redox. 1 hit. [Graphical view] |
| PRINTS | PR00353. 4FE4SFRDOXIN. |
| PROSITE | PS00198. 4FE4S_FER_1. 3 hits. PS51379. 4FE4S_FER_2. 4 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HDRA_METMP | ||||||||
| Accession | Primary (citable) accession number: Q6LWL2 | ||||||||
| Entry history |
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| 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


