Reviewed,
UniProtKB/Swiss-Prot P22658 (HOXF_RHOOP)
Last modified
June 16, 2009.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: NAD-reducing hydrogenase hoxS subunit alpha EC=1.12.1.2 | ||
| Gene names |
| ||
| Encoded on | Plasmid | ||
| Organism | Rhodococcus opacus (Nocardia opaca) | ||
| Taxonomic identifier | 37919 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus |
Protein attributes
| Sequence length | 37 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Subunits alpha and gamma of hoxS constitute an NADH--oxidoreductase. |
| Catalytic activity | H2 + NAD+ = H+ + NADH. |
| Cofactor | Binds 1 FMN Potential. Binds 1 4Fe-4S cluster Potential. |
| Subunit structure | Tetramer of an alpha and a gamma subunits (flavin-containing dimer), and a delta and a nickel-containing beta subunits (hydrogenase dimer). |
| Subcellular location | |
| Sequence similarities | Belongs to the complex I 51 kDa subunit family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | 4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing Plasmid |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen dehydrogenase activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Comparison of the NH2-terminal amino acid sequences of the four non-identical subunits of the NAD-linked hydrogenases from Nocardia opaca 1b and Alcaligenes eutrophus H16." Zaborosch C., Schneider K., Schlegel H.G., Kratzin H. Eur. J. Biochem. 181:175-180(1989) [PubMed: 2496982] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: 1B. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.12.1.2. 2206. |
Family and domain databases | |
| InterPro | IPR001949. NADH-UbQ_OxRdtase_51KDa_CS. [Graphical view] |
| ProDom | PD003859. Cmplx1_24kDa. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00644. COMPLEX1_51K_1. Partial match. PS00645. COMPLEX1_51K_2. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HOXF_RHOOP | ||||||||
| Accession | Primary (citable) accession number: P22658 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


