P00324 (FLAV_AZOVI) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 84.
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: Flavodoxin-2 | ||
| Gene names |
| ||
| Organism | Azotobacter vinelandii | ||
| Taxonomic identifier | 354 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter![]() |
Protein attributes
| Sequence length | 180 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Low-potential electron donor to a number of redox enzymes. NifF is the electron donor to nitrogenase. |
| Cofactor | FMN. |
| Subunit structure | Monomer. |
| Sequence similarities | Belongs to the flavodoxin family. Contains 1 flavodoxin-like domain. |
| Mass spectrometry | Molecular mass is 19533±5 Da from positions 2 - 180. Determined by ESI. Ref.4 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Nitrogen fixation Transport |
| Ligand | FMN Flavoprotein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrogen fixationInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | FMN binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: InterPro oxidoreductase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.3 Ref.4 | |||||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 180 | 179 | Flavodoxin-2 | PRO_0000171605 | ||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 4 – 173 | 170 | Flavodoxin-like | |||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 4 – 8 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 11 – 13 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 14 – 23 | 10 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 28 – 30 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 37 – 39 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 42 – 46 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 49 – 56 | 8 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 59 – 61 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 66 – 68 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 75 – 82 | 8 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 91 – 97 | 7 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 100 – 102 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 104 – 108 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 109 – 119 | 11 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 120 – 122 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 124 – 126 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 142 – 152 | 11 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 154 – 156 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 158 – 160 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 161 – 172 | 12 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 173 – 176 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii." Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R. J. Bacteriol. 171:1017-1027(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Isolation, sequencing, and mutagenesis of the nifF gene encoding flavodoxin from Azotobacter vinelandii." Bennett L., Jacobson M., Dean D.R. J. Biol. Chem. 263:1364-1369(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii." Tanaka M., Haniu M., Yasunobu K.T., Yoch D.C. Biochemistry 16:3525-3537(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-180. Strain: ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW. |
| [4] | "Flavodoxin 1 of Azotobacter vinelandii: characterization and role in electron donation to purified assimilatory nitrate reductase." Gangeswaran R., Eady R.R. Biochem. J. 317:103-108(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, MASS SPECTROMETRY. Strain: OP / UW136. |
| [5] | "Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding." Steensma E., Nijman M.J.M., Bollen Y.J.M., de Jager P.A., van den Berg W.A.M., van Dongen W.M.A.M., van Mierlo C.P.M. Protein Sci. 7:306-317(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR. Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M20568 Genomic DNA. Translation: AAA64735.1. J03519 Genomic DNA. Translation: AAA22154.1. | ||||||||||||
| PIR | FXAVEP. A29935. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P00324. | ||||||||||||
| SMR | P00324. Positions 2-180. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001094. Flavdoxin. IPR008254. Flavodoxin/NO_synth. IPR001226. Flavodoxin_CS. IPR010086. Flavodoxin_lc. [Graphical view] | ||||||||||||
| Pfam | PF00258. Flavodoxin_1. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF038996. FldA. 1 hit. | ||||||||||||
| PRINTS | PR00369. FLAVODOXIN. | ||||||||||||
| TIGRFAMs | TIGR01752. flav_long. 1 hit. | ||||||||||||
| PROSITE | PS00201. FLAVODOXIN. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P00324. | ||||||||||||
Entry information
| Entry name | FLAV_AZOVI | ||||||||
| Accession | Primary (citable) accession number: P00324 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
