Reviewed,
UniProtKB/Swiss-Prot Q93SN8 (PEBA_PROMP)
Last modified
May 5, 2009.
Version 44.
History...
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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: 15,16-dihydrobiliverdin:ferredoxin oxidoreductase EC=1.3.7.2 | ||||
| Gene names |
| ||||
| Organism | Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 59919 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus |
Protein attributes
| Sequence length | 236 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the two-electron reduction of biliverdin IX-alpha at the C15 methine bridge. HAMAP MF_00792 |
| Catalytic activity | 15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IX-alpha + reduced ferredoxin. HAMAP MF_00792 |
| Sequence similarities | Belongs to the HY2 family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Oxidoreductase |
| Technical term | 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 | 15,16-dihydrobiliverdin:ferredoxin oxidoreductase activity Inferred from electronic annotation. Source: HAMAP cobalt ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 236 | 236 | 15,16-dihydrobiliverdin:ferredoxin oxidoreductase HAMAP MF_00792 | PRO_0000216728 | |||||
Experimental info | |||||||||
| Sequence conflict | 47 | 1 | Q → R in AAK38141. Ref.1 | ||||||
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] | "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation." Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. Chisholm S.W.Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AY030300 Genomic DNA. Translation: AAK38141.1. BX548174 Genomic DNA. Translation: CAE20052.1. | |
| RefSeq | NP_893710.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1726360. |
| GenomeReviews | Gene locus PMM1593 in contig BX548174_GR. |
| KEGG | pmm:PMM1593. |
| NMPDR | fig|59919.1.peg.1589. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q93SN8. |
| OMA | Q93SN8. GFRRWRV. |
Enzyme and pathway databases | |
| BioCyc | PMAR167540:PMM1593-MON. |
Family and domain databases | |
| HAMAP | MF_00792. [Tree] |
| InterPro | IPR009249. Ferredoxin-dep_bilin_Rdtase. [Graphical view] |
| Pfam | PF05996. Fe_bilin_red. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PEBA_PROMP | ||||||||
| Accession | Primary (citable) accession number: Q93SN8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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