P22317 (HOXF_CUPNH) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 99.
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: NAD-reducing hydrogenase hoxS subunit alpha EC=1.12.1.2 | ||||
| Gene names |
| ||||
| Encoded on | Plasmid megaplasmid pHG1 | ||||
| Organism | Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 381666 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus |
Protein attributes
| Sequence length | 602 AA. |
| Sequence status | Complete. |
| 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 subunit (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 | Complete proteome Direct protein sequencing Plasmid |
| Gene Ontology (GO) | |
| 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 FMN bindingInferred from electronic annotation. Source: InterPro NAD bindingInferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activityInferred from electronic annotation. Source: InterPro hydrogen dehydrogenase activityInferred from electronic annotation. Source: EC metal 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 – 602 | 602 | NAD-reducing hydrogenase hoxS subunit alpha | PRO_0000118564 | |||||
Regions | |||||||||
| Nucleotide binding | 219 – 228 | 10 | NAD By similarity | ||||||
| Nucleotide binding | 332 – 379 | 48 | FMN By similarity | ||||||
Sites | |||||||||
| Metal binding | 499 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 502 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 505 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 545 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 24 | 1 | W → G AA sequence Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16." Tran-Betcke A., Warnecke U., Boecker C., Zaborosch C., Friedrich B. J. Bacteriol. 172:2920-2929(1990) [PubMed: 2188945] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis." Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G. J. Mol. Biol. 332:369-383(2003) [PubMed: 12948488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337. |
| [3] | "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 OF 1-27. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M55230 Genomic DNA. Translation: AAC06140.1. AY305378 Genomic DNA. Translation: AAP85841.1. |
| PIR | A35385. |
| RefSeq | NP_942727.1. NC_005241.1. |
3D structure databases | |
| ProteinModelPortal | P22317. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P22317. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2656814. |
| GenomeReviews | Gene locus PHG088 in contig AY305378_GR. |
| KEGG | reh:PHG088. |
| PATRIC | 35228786. VBIRalEut6770_0065. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1894. |
| HOGENOM | HBG669338. |
| OMA | FCTPCRV. |
| PhylomeDB | P22317. |
| ProtClustDB | CLSK923807. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:HOXFALCA-MONOMER. REUT381666:PHG088-MONOMER. |
| BRENDA | 1.12.1.2. 7290. |
Family and domain databases | |
| InterPro | IPR001949. NADH-UbQ_OxRdtase_51kDa_CS. IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd. IPR002023. NADH_UbQ_OxRdtase_24kDa_su. IPR011538. NADH_UbQ_OxRdtase_51kDa_su. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| KO | K00436. |
| Pfam | PF01257. Complex1_24kDa. 1 hit. PF01512. Complex1_51K. 1 hit. PF10589. NADH_4Fe-4S. 1 hit. [Graphical view] |
| SMART | SM00928. NADH_4Fe-4S. 1 hit. [Graphical view] |
| SUPFAM | SSF52833. Thiordxn-like_fd. 1 hit. |
| PROSITE | PS00644. COMPLEX1_51K_1. 1 hit. PS00645. COMPLEX1_51K_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HOXF_CUPNH | ||||||||
| Accession | Primary (citable) accession number: P22317 | ||||||||
| 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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