Reviewed,
UniProtKB/Swiss-Prot Q93TN0 (PCYA_ANASP)
Last modified
November 25, 2008.
Version 37.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Phycocyanobilin:ferredoxin oxidoreductase EC=1.3.7.5 | ||||
| Gene names |
| ||||
| Organism | Anabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 103690 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc |
Protein attributes
| Sequence length | 245 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin. |
| Catalytic activity | (3Z)-phycocyanobilin + oxidized ferredoxin = biliverdin IX-alpha + reduced ferredoxin. |
| Sequence similarities | Belongs to the HY2 family. |
Ontologies
Keywords | |
|---|---|
| Molecular function | Oxidoreductase |
| Technical term | 3D-structure Complete proteome |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW phytochromobilin biosynthetic processInferred from electronic annotation. Source: InterPro |
| Molecular function | cobalt ion binding Inferred from electronic annotation. Source: InterPro phycocyanobilin:ferredoxin oxidoreductase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 245 | 245 | Phycocyanobilin:ferredoxin oxidoreductase | PRO_0000216738 | ||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 9 – 12 | 4 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 15 – 31 | 17 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 41 – 43 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 44 – 50 | 7 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 53 – 63 | 11 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 65 – 77 | 13 | ||||||||||||||||||||||||||||||||||||||||
| Turn | 78 – 80 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 81 – 90 | 10 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 98 – 105 | 8 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 110 – 118 | 9 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 128 – 135 | 8 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 143 – 145 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 150 – 154 | 5 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 160 – 162 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 167 – 190 | 24 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 196 – 216 | 21 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 219 – 227 | 9 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 229 – 238 | 10 | ||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms." Frankenberg N., Mukougawa K., Kohchi T., Lagarias J.C. Plant Cell 13:965-978(2001) [PubMed: 11283349] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. Tabata S.DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF339056 Genomic DNA. Translation: AAK38587.1. BA000019 Genomic DNA. Translation: BAB75406.1. | |||||||||||||
| PIR | AD2269. | ||||||||||||
| RefSeq | NP_487747.1. | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1107305. | ||||||||||||
| GenomeReviews | Gene locus alr3707 in contig BA000019_GR. | ||||||||||||
| KEGG | ana:alr3707. | ||||||||||||
| NMPDR | fig|103690.1.peg.4014. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | Q93TN0. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | NSP103690:ALR3707-MON. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00618. [Tree] | ||||||||||||
| InterPro | IPR009249. Fe_bilin_red. [Graphical view] | ||||||||||||
| Pfam | PF05996. Fe_bilin_red. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | PCYA_ANASP | ||||||||
| Accession | Primary (citable) accession number: Q93TN0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


