Reviewed,
UniProtKB/Swiss-Prot P43101 (NIA_CICIN)
Last modified
November 25, 2008.
Version 64.
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: Nitrate reductase [NADH] Short name=NR EC=1.7.1.1 | ||
| Gene names |
| ||
| Organism | Cichorium intybus (Chicory) | ||
| Taxonomic identifier | 13427 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Cichorioideae › Cichorieae › Cichorium |
Protein attributes
| Sequence length | 920 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. |
| Catalytic activity | Nitrite + NAD(+) + H(2)O = nitrate + NADH. |
| Cofactor | Binds 1 FAD per subunit. Binds 1 heme group per subunit. Binds 1 molybdenum-pterin group per subunit. |
| Subunit structure | Homodimer By similarity. |
| Tissue specificity | In cortical cells of roots grown at low nitrate concentrations, in vascular tissues of roots at high nitrate concentrations and in root apex under both conditions. |
| Sequence similarities | Belongs to the nitrate reductase family. Contains 1 cytochrome b5 heme-binding domain. Contains 1 FAD-binding FR-type domain. |
Ontologies
Keywords | |
|---|---|
| Biological process | Nitrate assimilation |
| Ligand | FAD Flavoprotein Heme Iron Metal-binding Molybdenum NAD |
| Molecular function | Oxidoreductase |
Gene Ontology (GO) | |
| Biological process | nitrate assimilation Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: InterPro molybdenum ion bindingInferred from electronic annotation. Source: InterPro nitrate reductase (NADH) 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 – 920 | 920 | Nitrate reductase [NADH] | PRO_0000166054 | |||||
Regions | |||||||||
| Domain | 534 – 609 | 76 | Cytochrome b5 heme-binding | ||||||
| Domain | 663 – 775 | 113 | FAD-binding FR-type | ||||||
Sites | |||||||||
| Metal binding | 185 | 1 | Molybdenum-pterin Potential | ||||||
| Metal binding | 239 | 1 | Molybdenum-pterin Potential | ||||||
| Metal binding | 569 | 1 | Iron (heme axial ligand) By similarity | ||||||
| Metal binding | 592 | 1 | Iron (heme axial ligand) By similarity | ||||||
Amino acid modifications | |||||||||
| Disulfide bond | 424 | Interchain Potential | |||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Evidence for the nitrate-dependent spatial regulation of the nitrate reductase gene in chicory roots." Palms B., Goupil P., de Almeida Engler J., Van der Straeten D., Van Montagu M., Rambour S. Planta 200:20-27(1996) [PubMed: 8987617] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: cv. Witloof. Tissue: Leaf and Root. |
Cross-references
Sequence databases | |
|---|---|
| X84103 Genomic DNA. Translation: CAA58909.1. X84102 mRNA. Translation: CAA58908.1. | |
| PIR | S52301. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2CND based on UniProtKB P17571. |
| SMR | P43101. Positions 665-920. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR001199. Cyt_B5. IPR001834. Cyt_B5_reductase. IPR001709. FPN_cyt_redctse. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. IPR012137. Nitr_rd_NADH. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR000572. OxRdtase_Mopterin-bd. [Graphical view] |
| Gene3D | G3DSA:3.10.120.10. Cyt_B5. 1 hit. G3DSA:2.60.40.650. MoCF_oxrdtse_dimer. 1 hit. G3DSA:3.90.420.10. Oxred_molyb_bd. 1 hit. |
| Pfam | PF00173. Cyt-b5. 1 hit. PF00970. FAD_binding_6. 1 hit. PF03404. Mo-co_dimer. 1 hit. PF00175. NAD_binding_1. 1 hit. PF00174. Oxidored_molyb. 1 hit. [Graphical view] |
| PIRSF | PIRSF000233. Nitr_rd_NADH. 1 hit. |
| PRINTS | PR00406. CYTB5RDTASE. PR00363. CYTOCHROMEB5. PR00407. EUMOPTERIN. PR00371. FPNCR. |
| ProDom | PD000612. Cyt_B5. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. PS51384. FAD_FR. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NIA_CICIN | ||||||||
| Accession | Primary (citable) accession number: P43101 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


