ID CYF_MASLA Reviewed; 333 AA. AC P83793; Q5YJJ7; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 2. DT 28-JUN-2023, entry version 90. DE RecName: Full=Cytochrome f; DE Flags: Precursor; GN Name=petA; OS Mastigocladus laminosus (Fischerella sp.). OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae; OC Mastigocladus. OX NCBI_TaxID=83541; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Yan J., Zhang H., Cramer W.A.; RT "Cloning and characterization of the petBD and petCA operon from the RT thermophilic cyanobacterium Mastigocladus laminosus."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH HEME IN CYTOCHROME RP B6-F COMPLEX, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND RP TOPOLOGY. RX PubMed=14526088; DOI=10.1126/science.1090165; RA Kurisu G., Zhang H., Smith J.L., Cramer W.A.; RT "Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning RT the cavity."; RL Science 302:1009-1014(2003). 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 {ECO:0000305|PubMed:14526088}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000269|PubMed:14526088}; CC Note=Binds 1 heme group covalently. {ECO:0000269|PubMed:14526088}; 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. {ECO:0000269|PubMed:14526088}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane CC {ECO:0000269|PubMed:14526088}; Single-pass membrane protein CC {ECO:0000269|PubMed:14526088}. CC -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY390356; AAR26241.1; -; Genomic_DNA. DR PDB; 1VF5; X-ray; 3.00 A; C/P=45-333. DR PDB; 2D2C; X-ray; 3.80 A; C/P=45-333. DR PDB; 2E74; X-ray; 3.00 A; C=45-333. DR PDB; 2E75; X-ray; 3.55 A; C=45-333. DR PDB; 2E76; X-ray; 3.41 A; C=45-333. DR PDB; 4H0L; X-ray; 3.25 A; C=45-333. DR PDB; 4H13; X-ray; 3.07 A; C=45-333. DR PDB; 4I7Z; X-ray; 2.80 A; C=45-333. DR PDB; 4PV1; X-ray; 3.00 A; C=45-333. DR PDBsum; 1VF5; -. DR PDBsum; 2D2C; -. DR PDBsum; 2E74; -. DR PDBsum; 2E75; -. DR PDBsum; 2E76; -. DR PDBsum; 4H0L; -. DR PDBsum; 4H13; -. DR PDBsum; 4I7Z; -. DR PDBsum; 4PV1; -. DR AlphaFoldDB; P83793; -. DR SMR; P83793; -. DR DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide. DR DrugBank; DB04646; Dibromothymoquinone. DR EvolutionaryTrace; P83793; -. DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule. DR Gene3D; 2.40.50.100; -; 1. DR Gene3D; 2.60.40.830; Cytochrome f large domain; 1. DR Gene3D; 1.20.5.700; Single helix bin; 1. DR HAMAP; MF_00610; Cytb6_f_cytF; 1. DR InterPro; IPR024058; Cyt-f_TM. DR InterPro; IPR002325; Cyt_f. DR InterPro; IPR024094; Cyt_f_lg_dom. DR InterPro; IPR036826; Cyt_f_lg_dom_sf. DR InterPro; IPR011054; Rudment_hybrid_motif. DR PANTHER; PTHR33288; -; 1. DR PANTHER; PTHR33288:SF10; CYTOCHROME F; 1. DR Pfam; PF01333; Apocytochr_F_C; 1. DR Pfam; PF16639; Apocytochr_F_N; 1. DR PRINTS; PR00610; CYTOCHROMEF. DR SUPFAM; SSF103431; Cytochrome f subunit of the cytochrome b6f complex, transmembrane anchor; 1. DR SUPFAM; SSF49441; Cytochrome f, large domain; 1. DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1. DR PROSITE; PS51010; CYTF; 1. PE 1: Evidence at protein level; KW 3D-structure; Electron transport; Heme; Iron; Membrane; Metal-binding; KW Photosynthesis; Signal; Thylakoid; Transmembrane; Transmembrane helix; KW Transport. FT SIGNAL 1..37 FT /evidence="ECO:0000255" FT CHAIN 38..333 FT /note="Cytochrome f" FT /id="PRO_0000207977" FT TOPO_DOM 38..298 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:14526088" FT TRANSMEM 299..319 FT /note="Helical" FT /evidence="ECO:0000305|PubMed:14526088" FT TOPO_DOM 320..333 FT /note="Lumenal, thylakoid" FT /evidence="ECO:0000305|PubMed:14526088" FT BINDING 45 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 /evidence="ECO:0000269|PubMed:14526088" FT BINDING 66 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:14526088" FT BINDING 69 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:14526088" FT BINDING 70 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 /evidence="ECO:0000269|PubMed:14526088" FT HELIX 46..52 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:2E74" FT HELIX 65..68 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 89..95 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 115..121 FT /evidence="ECO:0007829|PDB:4I7Z" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:4I7Z" FT HELIX 136..142 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 157..164 FT /evidence="ECO:0007829|PDB:4I7Z" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 169..176 FT /evidence="ECO:0007829|PDB:4I7Z" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 189..200 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 219..222 FT /evidence="ECO:0007829|PDB:1VF5" FT STRAND 227..230 FT /evidence="ECO:0007829|PDB:2E74" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 238..242 FT /evidence="ECO:0007829|PDB:2E74" FT STRAND 245..248 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:2E74" FT STRAND 255..259 FT /evidence="ECO:0007829|PDB:4I7Z" FT STRAND 283..293 FT /evidence="ECO:0007829|PDB:4I7Z" FT HELIX 296..328 FT /evidence="ECO:0007829|PDB:4I7Z" FT TURN 329..331 FT /evidence="ECO:0007829|PDB:2E76" SQ SEQUENCE 333 AA; 36450 MW; E768F5C264323061 CRC64; MRNSCKKARR TRPLKATIQA LLVAIATMTF FFTSDIALPQ SAAAYPFWAQ QTYPETPREP TGRIVCANCH LAAKPAEVEV PQSVLPDTVF KAVVKIPYDT KLQQVAADGS KVGLNVGAVL MLPEGFKIAP EERIPEELKK EVGDVYFQPY KEGQDNVLLV GPLPGEQYQE IVFPVLSPNP TTDKNIHFGK YAIHLGANRG RGQIYPTGEK SNNNVFTASA TGTITKIAKE EDEYGNVKYQ VSIQTDSGKT VVDTIPAGPE LIVSEGQAVK AGEALTNNPN VGGFGQDDTE IVLQDPNRVK WMIAFICLVM LAQLMLILKK KQVEKVQAAE MNF //