Reviewed,
UniProtKB/Swiss-Prot P83791 (CYB6_MASLA)
Last modified
March 3, 2009.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cytochrome b6 | ||
| Gene names |
| ||
| Organism | Mastigocladus laminosus (Fischerella sp.) | ||
| Taxonomic identifier | 83541 [NCBI] | ||
| Taxonomic lineage | Bacteria › Cyanobacteria › Stigonematales › Mastigocladus |
Protein attributes
| Sequence length | 215 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. HAMAP MF_00633 |
| Cofactor | Binds 2 heme groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently. Ref.1 |
| Subunit structure | The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer. HAMAP MF_00633 |
| Subcellular location | Cellular thylakoid membrane; Multi-pass membrane protein. HAMAP MF_00633 |
| Miscellaneous | Heme 1 (or BH or b566) is high-potential and absorbs at about 566 nm, and heme 2 (or BL or b562) is low-potential and absorbs at about 562 nm By similarity. |
| Sequence similarities | Belongs to the cytochrome b family. PetB subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Photosynthesis Transport |
| Cellular component | Membrane Thylakoid |
| Domain | Transmembrane |
| Ligand | Heme Iron Metal-binding |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | photosynthesis Inferred from electronic annotation. Source: HAMAP respiratory electron transport chainInferred from electronic annotation. Source: InterPro transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW thylakoid membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity Inferred from electronic annotation. Source: HAMAP iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW 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 | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 215 | 215 | Cytochrome b6 HAMAP MF_00633 | PRO_0000061827 | |||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||
| Transmembrane | 32 – 52 | 21 | Potential | ||||||||||||||||||||||||||||||||||
| Transmembrane | 90 – 110 | 21 | Potential | ||||||||||||||||||||||||||||||||||
| Transmembrane | 116 – 136 | 21 | Potential | ||||||||||||||||||||||||||||||||||
| Transmembrane | 186 – 206 | 21 | Potential | ||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||
| Metal binding | 86 | 1 | Iron (heme 2 axial ligand) HAMAP MF_00633 | ||||||||||||||||||||||||||||||||||
| Metal binding | 100 | 1 | Iron (heme 1 axial ligand) HAMAP MF_00633 | ||||||||||||||||||||||||||||||||||
| Metal binding | 187 | 1 | Iron (heme 2 axial ligand) HAMAP MF_00633 | ||||||||||||||||||||||||||||||||||
| Metal binding | 202 | 1 | Iron (heme 1 axial ligand) HAMAP MF_00633 | ||||||||||||||||||||||||||||||||||
| Binding site | 35 | 1 | Heme 1 (covalent; via 1 link) HAMAP MF_00633 | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Helix | 4 – 12 | 9 | |||||||||||||||||||||||||||||||||||
| Helix | 33 – 35 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 36 – 54 | 19 | |||||||||||||||||||||||||||||||||||
| Turn | 55 – 57 | 3 | |||||||||||||||||||||||||||||||||||
| Turn | 62 – 64 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 65 – 73 | 9 | |||||||||||||||||||||||||||||||||||
| Helix | 79 – 106 | 28 | |||||||||||||||||||||||||||||||||||
| Beta strand | 109 – 113 | 5 | |||||||||||||||||||||||||||||||||||
| Helix | 116 – 135 | 20 | |||||||||||||||||||||||||||||||||||
| Turn | 136 – 139 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 142 – 152 | 11 | |||||||||||||||||||||||||||||||||||
| Helix | 154 – 156 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 161 – 170 | 10 | |||||||||||||||||||||||||||||||||||
| Beta strand | 172 – 175 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 178 – 188 | 11 | |||||||||||||||||||||||||||||||||||
| Helix | 190 – 204 | 15 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: cytochrome b(6)f complex from spinach and the cyanobacterium Mastigocladus laminosus." Whitelegge J.P., Zhang H., Aguilera R., Taylor R.M., Cramer W.A. Mol. Cell. Proteomics 1:816-827(2002) [PubMed: 12438564] [Abstract] Cited for: HEME-BINDING. |
| [2] | "Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity." Kurisu G., Zhang H., Smith J.L., Cramer W.A. Science 302:1009-1014(2003) [PubMed: 14526088] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), METAL-BINDING SITES. |
| + | Additional computationally mapped references. |
Cross-references
3D structure databases | |||||||||||||||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||
| HAMAP | MF_00633. [Tree] | ||||||||||||||||||||||||||||||||||||
| InterPro | IPR016175. Cyt_b/b6. IPR005797. Cyt_b/b6_N. [Graphical view] | ||||||||||||||||||||||||||||||||||||
| Gene3D | G3DSA:1.20.810.10. Cytochrome_b/b6. 1 hit. | ||||||||||||||||||||||||||||||||||||
| PANTHER | PTHR19271. Cytochrome_b/b6. 1 hit. | ||||||||||||||||||||||||||||||||||||
| Pfam | PF00033. Cytochrom_B_N. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||
| PROSITE | PS51002. CYTB_NTER. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | CYB6_MASLA | ||||||||
| Accession | Primary (citable) accession number: P83791 | ||||||||
| 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


