Reviewed,
UniProtKB/Swiss-Prot P22944 (NIR_EMENI)
Last modified
June 16, 2009.
Version 71.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Nitrite reductase [NAD(P)H] EC=1.7.1.4 | ||||
| Gene names |
| ||||
| Organism | Emericella nidulans (Aspergillus nidulans) | ||||
| Taxonomic identifier | 162425 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella |
Protein attributes
| Sequence length | 1104 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Ammonium hydroxide + 3 NAD(P)+ + H2O = nitrite + 3 NAD(P)H. |
| Cofactor | Binds 1 siroheme per subunit. Binds 1 4Fe-4S cluster per subunit By similarity. FAD. Binds 1 2Fe-2S cluster per subunit By similarity. |
| Pathway | |
| Subunit structure | Homodimer. |
| Sequence similarities | Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. Contains 1 Rieske domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nitrate assimilation |
| Ligand | 2Fe-2S 4Fe-4S FAD Flavoprotein Heme Iron Iron-sulfur Metal-binding NADP |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster bindingInferred from electronic annotation. Source: UniProtKB-KW FAD bindingInferred from electronic annotation. Source: InterPro NADP or NADPH bindingInferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro nitrite reductase [NAD(P)H] 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 – 1104 | 1104 | Nitrite reductase [NAD(P)H] | PRO_0000199958 | |||||
Regions | |||||||||
| Domain | 932 – 1040 | 109 | Rieske | ||||||
| Nucleotide binding | 44 – 79 | 36 | FAD Potential | ||||||
| Nucleotide binding | 146 – 176 | 31 | NAD or NADP Potential | ||||||
Sites | |||||||||
| Metal binding | 720 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 726 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 760 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 764 | 1 | Iron (siroheme axial ligand) By similarity | ||||||
| Metal binding | 764 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 976 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 978 | 1 | Iron-sulfur (2Fe-2S); via pros nitrogen By similarity | ||||||
| Metal binding | 1001 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 1004 | 1 | Iron-sulfur (2Fe-2S); via pros nitrogen By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 709 | 1 | A → R in AAA33315. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and characterisation of the crnA-niiA-niaD gene cluster for nitrate assimilation in Aspergillus nidulans." Johnstone I.L., McCabe P.C., Greaves P., Gurr S.J., Cole G.E., Brow M.A.D., Unkles S.E., Clutterbuck A.J., Kinghorn J.R., Innis M.A. Gene 90:181-192(1990) [PubMed: 2205530] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H.  Birren B.W.Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4. |
Cross-references
Sequence databases | |
|---|---|
| M58289 Genomic DNA. Translation: AAA33315.1. AACD01000015 Genomic DNA. Translation: EAA65575.1. | |
| PIR | JH0181. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FQT based on UniProtKB P37332. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.7.1.4. 3859. |
Family and domain databases | |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00365. NIR_SIR. 1 hit. PS51296. RIESKE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NIR_EMENI | ||||||||
| Accession | Primary (citable) accession number: P22944 Secondary accession number(s): Q5BEM3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
