HAMAP rule MF_00633
General rule information
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Accession | MF_00633 |
Dates | 4-APR-2003 (Created) 17-FEB-2023 (Last updated, Version 54) |
Name | Cytb6_f_cytb6 |
Scope | Bacteria; Cyanobacteriota
Bacteria; Heliobacteriaceae
Plastid |
Templates | Q00471 (CYB6_CHLRE); P00165 (CYB6_SPIOL): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
Protein name |
|
case not <OC:Heliobacteriaceae>
Gene name |
|
else case <OC:Heliobacteriaceae>
Gene name |
|
end case
Comments
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case <OC:Heliobacteriaceae>
Function | Component of the cytochrome bc complex which donates electrons to the photosynthetic reaction center. |
Cofactor | heme Note: Binds 2 heme groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently. |
Subunit | The subunits of the cytochrome bc complex are a Rieske Fe-S protein (PetC), cytochrome b6 (PetB), subunit IV (PetD), and a diheme cytochrome c (PetX). |
else case not <OC:Heliobacteriaceae>
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. |
Cofactor | heme Note: Binds 2 heme groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently. |
Subunit | 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. |
end case
case <OC:Heliobacteriaceae>
Subcellular location | Cell membrane; Multi-pass membrane protein. |
else case <OG:Chloroplast>
Subcellular location | Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. |
else case <OC:Gloeobacter>
Subcellular location | Cell inner membrane; Multi-pass membrane protein. |
else
Subcellular location | Cellular thylakoid membrane; Multi-pass membrane protein. |
end case
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. |
Similarity | Belongs to the cytochrome b family. PetB subfamily. |
Keywords
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case <OC:Gloeobacter>
else case <OG:Chloroplast> or <Property:Thylakoid>
else case <OC:Heliobacteriaceae>
end case
Gene Ontology
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case <OC:Heliobacteriaceae> or <OC:Gloeobacter>
GO:0005886; Cellular component: plasma membrane.
else case <OG:Chloroplast>
GO:0009535; Cellular component: chloroplast thylakoid membrane.
else
GO:0042651; Cellular component: thylakoid membrane.
end case
GO:0045158; Molecular function: electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity.
GO:0015979; Biological process: photosynthesis.
GO:0015979; Biological process: photosynthesis.
Cross-references
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Features
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From: CYB6_ARATH (P56773) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
TRANSMEM | 32 | 52 | Helical | |||||||||
TRANSMEM | 90 | 110 | Helical | |||||||||
TRANSMEM | 116 | 136 | Helical | |||||||||
TRANSMEM | 186 | 206 | Helical | |||||||||
BINDING | 86 | 86 | /ligand="heme" /ligand_id="ChEBI:CHEBI:30413" /ligand_label="2" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue | H | ||||||||
BINDING | 100 | 100 | /ligand="heme" /ligand_id="ChEBI:CHEBI:30413" /ligand_label="1" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue | H | ||||||||
BINDING | 187 | 187 | /ligand="heme" /ligand_id="ChEBI:CHEBI:30413" /ligand_label="2" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue | H | ||||||||
BINDING | 202 | 202 | /ligand="heme" /ligand_id="ChEBI:CHEBI:30413" /ligand_label="1" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue | H | ||||||||
BINDING | 35 | 35 | /ligand="heme" /ligand_id="ChEBI:CHEBI:30413" /ligand_label="1" /note="covalent | C |
Additional information
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Size range | 213-222 amino acids |
Related rules | None |
Fusion | None |
Comments | In maize and tobacco position 204 has been shown to undergo RNA editing to change the codon from Pro to Leu. It has therefore been suggested to occur in all other plants where this codon is Pro (CCA -> CTA). In C.reinhardtii an engineered Pro mutation at this position is unable to assemble intact complex, giving strength to this suggestion. |