Reviewed,
UniProtKB/Swiss-Prot P80509 (HC3L_THIFE)
Last modified
November 4, 2008.
Version 30.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information
Names and origin
| Protein names | Recommended name: Cytochrome c3 hydrogenase large chain Short name=Hydrogenase EC=1.12.2.1 | ||
| Gene names |
| ||
| Organism | Thiobacillus ferrooxidans (Acidithiobacillus ferrooxidans) | ||
| Taxonomic identifier | 920 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus |
Protein attributes
| Sequence length | 122 AA. |
| Sequence status | Fragments. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 2 H(2) + ferricytochrome c3 = 4 H(+) + ferrocytochrome c3. |
| Cofactor | Iron. |
| Caution | The order of the peptides shown is uncertain. It is also unknown if gaps exist between the peptides. |
Ontologies
Keywords | |
|---|---|
| Ligand | Iron |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | cytochrome-c3 hydrogenase activity Inferred from electronic annotation. Source: EC 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 – ›122 | ›122 | Cytochrome c3 hydrogenase large chain | PRO_0000083913 | |||||
Experimental info | |||||||||
| Non-adjacent residues | 20 – 21 | 2 | |||||||
| Non-adjacent residues | 29 – 30 | 2 | |||||||
| Non-adjacent residues | 35 – 36 | 2 | |||||||
| Non-adjacent residues | 42 – 43 | 2 | |||||||
| Non-adjacent residues | 59 – 60 | 2 | |||||||
| Non-adjacent residues | 72 – 73 | 2 | |||||||
| Non-adjacent residues | 78 – 79 | 2 | |||||||
| Non-adjacent residues | 87 – 88 | 2 | |||||||
| Non-adjacent residues | 98 – 99 | 2 | |||||||
| Non-adjacent residues | 107 – 108 | 2 | |||||||
| Non-terminal residue | 122 | 1 | |||||||
Sequences
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References
| [1] | "Purification and characterization of the hydrogenase from Thiobacillus ferrooxidans." Fischer J., Quentmeier A., Kostka S., Kraft R., Friedrich C.G. Arch. Microbiol. 165:289-296(1996) [PubMed: 8661919] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: ATCC 19859 / NCIB 9490. |
Cross-references
Entry information
| Entry name | HC3L_THIFE | ||||||||
| Accession | Primary (citable) accession number: P80509 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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