CYC6_SYNEL
ID CYC6_SYNEL Reviewed; 87 AA.
AC P0A3Y0; P56534; Q9F1M0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Cytochrome c6;
DE AltName: Full=Cytochrome c-553;
DE AltName: Full=Cytochrome c553;
DE AltName: Full=Soluble cytochrome f;
GN Name=petJ;
OS Synechococcus elongatus.
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=32046;
RN [1]
RP STRUCTURE BY NMR IN COMPLEX WITH HEME, AND COFACTOR.
RX PubMed=9427738; DOI=10.1093/emboj/17.1.27;
RA Beissinger M., Sticht H., Sutter M., Ejchart A., Haehnel W., Roesch P.;
RT "Solution structure of cytochrome c6 from the thermophilic cyanobacterium
RT Synechococcus elongatus.";
RL EMBO J. 17:27-36(1998).
CC -!- FUNCTION: Functions as an electron carrier between membrane-bound
CC cytochrome b6-f and photosystem I in oxygenic photosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid lumen {ECO:0000305}.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC {ECO:0000269|PubMed:9427738}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.
CC {ECO:0000305}.
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DR PDB; 1C6S; NMR; -; A=1-87.
DR PDBsum; 1C6S; -.
DR AlphaFoldDB; P0A3Y0; -.
DR SMR; P0A3Y0; -.
DR EvolutionaryTrace; P0A3Y0; -.
DR GO; GO:0031979; C:plasma membrane-derived thylakoid lumen; 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; 1.10.760.10; -; 1.
DR HAMAP; MF_00594; Cytc_PetJ; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR023655; Cyt_C6.
DR InterPro; IPR008168; Cyt_C_IC.
DR PANTHER; PTHR34688; PTHR34688; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Metal-binding;
KW Photosynthesis; Thylakoid; Transport.
FT CHAIN 1..87
FT /note="Cytochrome c6"
FT /id="PRO_0000208687"
FT BINDING 14
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9427738"
FT BINDING 17
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9427738"
FT BINDING 18
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00594,
FT ECO:0000305|PubMed:9427738"
FT BINDING 58
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00594,
FT ECO:0000305|PubMed:9427738"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:1C6S"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1C6S"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:1C6S"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1C6S"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1C6S"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1C6S"
FT TURN 34..38
FT /evidence="ECO:0007829|PDB:1C6S"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:1C6S"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1C6S"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1C6S"
SQ SEQUENCE 87 AA; 9178 MW; 15213EC6404D1C64 CRC64;
ADLANGAKVF SGNCAACHMG GGNVVMANKT LKKEALEQFG MYSEDAIIYQ VQHGKNAMPA
FAGRLTDEQI QDVAAYVLDQ AAKGWAG
