P60227 (MVHA_METTM) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 26.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: F420-non-reducing hydrogenase subunit A EC=1.12.99.- Alternative name(s): Methyl viologen-reducing hydrogenase subunit alpha Short name=MVH subunit A | ||||
| Gene names |
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| Organism | Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 79929 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter |
Protein attributes
| Sequence length | 472 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 provides reducing equivalents for heterodisulfide reductase. Ref.3 |
| Cofactor | Nickel Potential. |
| Subunit structure | The F420-non-reducing hydrogenase is composed of three subunits; mvhA, mvhD and mvhG. It forms a complex with the heterodisulfide reductase (hdr). Ref.2 |
| Sequence similarities | Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Nickel |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular function | ferredoxin hydrogenase activity Inferred from electronic annotation. Source: InterPro nickel cation bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||
| Chain | 2 – 472 | 471 | F420-non-reducing hydrogenase subunit A | PRO_0000199727 | |||||
Sites | |||||||||
| Metal binding | 61 | 1 | Nickel Potential | ||||||
| Metal binding | 64 | 1 | Nickel Potential | ||||||
| Metal binding | 442 | 1 | Nickel Potential | ||||||
| Metal binding | 445 | 1 | Nickel Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 11 | 1 | R → L AA sequence Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism." Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K. J. Bacteriol. 192:5850-5851(2010) [PubMed: 20802048] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg. |
| [2] | "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: PROTEIN SEQUENCE OF 2-18, SUBUNIT, ASSOCIATION WITH HETERODISULFIDE REDUCTASE. Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg. |
| [3] | "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: FUNCTION, ASSOCIATION WITH HETERODISULFIDE REDUCTASE. Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001710 Genomic DNA. Translation: ADL59096.1. |
| RefSeq | YP_003850409.1. NC_014408.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 9705226. |
| GenomeReviews | Gene locus MTBMA_c15170 in contig CP001710_GR. |
| KEGG | mmg:MTBMA_c15170. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | EVRGFEK. |
Family and domain databases | |
| InterPro | IPR001501. Ni-dep_hyd_lsu. IPR018194. Ni-dep_hyd_lsu_Ni_BS. [Graphical view] |
| KO | K14126. |
| Pfam | PF00374. NiFeSe_Hases. 2 hits. [Graphical view] |
| PROSITE | PS00507. NI_HGENASE_L_1. 1 hit. PS00508. NI_HGENASE_L_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MVHA_METTM | ||||||||
| Accession | Primary (citable) accession number: P60227 Secondary accession number(s): D9PXZ8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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