P85098 (NARH_BRASZ) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 28, 2012.
Version 24.
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: Respiratory nitrate reductase beta chain EC=1.7.99.4 Alternative name(s): Respiratory membrane-bound nitrate reductase subunit beta | ||
| Gene names |
| ||
| Organism | Bradyrhizobium sp. | ||
| Taxonomic identifier | 376 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium![]() |
Protein attributes
| Sequence length | 266 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | The nitrate reductase enzyme complex allows Bradyrhizobium sp. USDA 3045 to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit. Ref.1 UniProtKB P11349 |
| Catalytic activity | Nitrite + acceptor = nitrate + reduced acceptor. Ref.1 |
| Cofactor | Binds 3 4Fe-4S clusters per subunit By similarity. UniProtKB P11349 Binds 1 3Fe-4S cluster per subunit By similarity. UniProtKB P11349 |
| Enzyme regulation | Inhibited by micromolar concentrations of azide. Ref.1 |
| Subunit structure | Heterotrimer composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane. Ref.1 |
| Subcellular location | |
| Induction | Induced by anaerobiosis, there is no significant expression in an aerobic environment. Expression is further induced in the presence of nitrate or nitrite. Ref.1 |
| Sequence similarities | Contains at least 2 4Fe-4S ferredoxin-type domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Nitrate assimilation Transport |
| Cellular component | Cell membrane Cytoplasm Membrane |
| Domain | Repeat |
| Ligand | 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilationInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster bindingInferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW nitrate reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›266 | ›266 | Respiratory nitrate reductase beta chain | PRO_0000283779 | |||||
Regions | |||||||||
| Domain | 3 – 32 | 30 | 4Fe-4S ferredoxin-type 1 | ||||||
| Domain | 30 – 61 | 32 | 4Fe-4S ferredoxin-type 2 | ||||||
Sites | |||||||||
| Metal binding | 12 | 1 | Iron-sulfur 1 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 15 | 1 | Iron-sulfur 1 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 18 | 1 | Iron-sulfur 1 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 22 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 39 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 42 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 47 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 51 | 1 | Iron-sulfur 4 (3Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 73 | 1 | Iron-sulfur 4 (3Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 77 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 81 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 84 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 96 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
| Metal binding | 100 | 1 | Iron-sulfur 1 (4Fe-4S) By similarity UniProtKB P11349 | ||||||
Experimental info | |||||||||
| Non-adjacent residues | 11 – 12 | 2 | |||||||
| Non-adjacent residues | 23 – 24 | 2 | |||||||
| Non-adjacent residues | 37 – 38 | 2 | |||||||
| Non-adjacent residues | 58 – 59 | 2 | |||||||
| Non-adjacent residues | 71 – 72 | 2 | |||||||
| Non-adjacent residues | 80 – 81 | 2 | |||||||
| Non-adjacent residues | 87 – 88 | 2 | |||||||
| Non-adjacent residues | 103 – 104 | 2 | |||||||
| Non-adjacent residues | 114 – 115 | 2 | |||||||
| Non-adjacent residues | 131 – 132 | 2 | |||||||
| Non-adjacent residues | 143 – 144 | 2 | |||||||
| Non-adjacent residues | 150 – 151 | 2 | |||||||
| Non-adjacent residues | 163 – 164 | 2 | |||||||
| Non-adjacent residues | 168 – 169 | 2 | |||||||
| Non-adjacent residues | 178 – 179 | 2 | |||||||
| Non-adjacent residues | 198 – 199 | 2 | |||||||
| Non-adjacent residues | 210 – 211 | 2 | |||||||
| Non-adjacent residues | 221 – 222 | 2 | |||||||
| Non-adjacent residues | 238 – 239 | 2 | |||||||
| Non-adjacent residues | 248 – 249 | 2 | |||||||
| Non-adjacent residues | 256 – 257 | 2 | |||||||
| Non-terminal residue | 266 | 1 | |||||||
Sequences
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References
| [1] | "Identification of membrane-bound respiratory nitrate reductase from Bradyrhizobium sp. (Lupinus) USDA 3045 by tandem mass spectrometry." Polcyn W. Submitted (FEB-2007) to UniProtKB Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION. Strain: USDA 3045. |
Cross-references
3D structure databases | |
|---|---|
| ProteinModelPortal | P85098. |
| SMR | P85098. Positions 1-256. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR017896. 4Fe4S_Fe-S-bd. [Graphical view] |
| Pfam | PF13247. Fer4_11. 1 hit. [Graphical view] |
| PROSITE | PS00198. 4FE4S_FER_1. False negative. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NARH_BRASZ | ||||||||
| Accession | Primary (citable) accession number: P85098 | ||||||||
| 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 |

Clusters with
