AC   MF_00610;
DC   Protein; auto
TR   HAMAP; MF_00610; -; 1; level=0
XX
Names: Cytb6_f_cytF
XX
ID   CYF
DE   RecName: Full=Cytochrome f;
DE   Flags: Precursor;
GN   Name=petA;
XX
CC   -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC       electron transfer between photosystem II (PSII) and photosystem I
CC       (PSI), cyclic electron flow around PSI, and state transitions.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC       Note=Binds 1 heme group covalently.;
CC   -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC       cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and
CC       the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and
CC       PetN. The complex functions as a dimer.
case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-
CC       pass membrane protein.
else case <OC:Gloeobacter>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC       protein.
else
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane
CC       protein.
end case
CC   -!- SIMILARITY: Belongs to the cytochrome f family.
XX
DR   Pfam; PF01333; Apocytochr_F_C; 1; trigger=no
DR   PRINTS; PR00610; CYTOCHROMEF; 1; trigger=no
DR   PROSITE; PS51010; CYTF; 1; trigger=no
DR   General; Signal; -; 1; trigger=yes
DR   General; Transmembrane; -; 1; trigger=yes
XX
KW   Transport
KW   Electron transport
KW   Heme
KW   Iron
KW   Metal-binding
case <OC:Gloeobacter>
KW   Cell membrane
KW   Cell inner membrane
else
KW   Thylakoid
end case
KW   Photosynthesis
KW   Membrane
KW   Transmembrane
KW   Signal
KW   Transmembrane helix
XX
GO   GO:0009055; F:electron transfer activity
GO   GO:0015979; P:photosynthesis
case <OG:Chloroplast>
GO   GO:0009535; C:chloroplast thylakoid membrane
else case <OC:Gloeobacter>
GO   GO:0005886; C:plasma membrane
else
GO   GO:0042651; C:thylakoid membrane
end case
XX
FT   From: CYF_BRARR (P36438)
FT   BINDING         36
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   Condition: [FY]
FT   BINDING         60
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   Condition: H
FT   BINDING         56
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT   Condition: C
FT   BINDING         59
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT   Condition: C
XX
Size: 300-342;
Related: None;
Template: P36438; P23577; P83793;
Scope:
 Bacteria; Cyanobacteriota
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: In LEPTE the N-terminus is unusually long, not used in seed
 alignment or size range. In GLOVI the first conserved heme axial ligand
 Phe or Tyr is a Trp, the sequence is designated atypical.
XX
# Revision 1.51 2023/02/17
//