HAMAP annotation rule: MF_00633
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Accession MF_00633
Dates 4-APR-2003 (Created)
2-DEC-2010 (Last updated, Version 46)
Data class Protein
Names Cytb6_f_cytb6



Identifier CYB6
Protein name
RecName: Full=Cytochrome b6;

case not <OC:Heliobacteriaceae>
Gene name petB

else case <OC:Heliobacteriaceae>
Gene name petB, cytB
end case


case <OC:Heliobacteriaceae>
FUNCTION: Component of the cytochrome bc complex which donates electrons to the photosynthetic reaction center (By similarity).
COFACTOR: Binds 2 heme groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently (By similarity).
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) (By similarity).

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 (By similarity).
COFACTOR: Binds 2 heme groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently (By similarity).
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 (By similarity).
end case


case <OC:Heliobacteriaceae>
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein (By similarity).

else case <OG:Chloroplast>
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein (By similarity).

else case <OC:Gloeobacter>
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein (By similarity).

else
SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein (By similarity).
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 (By similarity).
SIMILARITY: Belongs to the cytochrome b family. PetB subfamily.
Pfam PF00033; Cytochrom_B_N; 1;
PROSITE PS51002; CYTB_NTER; 1;

case <OC:Gloeobacter>

else case <OG:Chloroplast> or <Property:Thylakoid>

else case <OC:Heliobacteriaceae>
end case


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:0055114; Biological process: oxidation-reduction process.
From: CYB6_ARATH (P56773)
Key     From     To       Description   Condition   FTGroup
TRANSMEM     32     52       Helical; (Potential)      
TRANSMEM     90     110       Helical; (Potential)      
TRANSMEM     116     136       Helical; (Potential)      
TRANSMEM     186     206       Helical; (Potential)      
METAL     86     86       Iron (heme 2 axial ligand) (By similarity)   H  
METAL     100     100       Iron (heme 1 axial ligand) (By similarity)   H  
METAL     187     187       Iron (heme 2 axial ligand) (By similarity)   H  
METAL     202     202       Iron (heme 1 axial ligand) (By similarity)   H  
BINDING     35     35       Heme 1 (covalent; via 1 link) (By similarity)   C  



Size range: 213-222 amino acids
Related UniRules: None
Template: Q00471 (CYB6_CHLRE); P00165 (CYB6_SPIOL): [Recover all]
Scope: Bacteria; Cyanobacteria
Bacteria; Heliobacteriaceae
Plastid
Fusion: Nter: None; Cter: None
Duplicate: None
Plasmid encoded: 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.

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