ID   CYC6_APHFL              Reviewed;          87 AA.
AC   P00116;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 97.
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   Aphanizomenon flos-aquae.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Aphanizomenon.
OX   NCBI_TaxID=1176;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6286617; DOI=10.1016/s0021-9258(18)34077-8;
RA   Ulrich E.L., Krogmann D.W., Markley J.L.;
RT   "Structure and heme environment of ferrocytochrome c553 from 1H NMR
RT   studies.";
RL   J. Biol. Chem. 257:9356-9364(1982).
CC   -!- FUNCTION: Functions as an electron carrier between membrane-bound
CC       cytochrome b6-f and photosystem I in oxygenic photosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid lumen {ECO:0000305}.
CC   -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.
CC       {ECO:0000305}.
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DR   PIR; A00108; CCFZ6.
DR   AlphaFoldDB; P00116; -.
DR   SMR; P00116; -.
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; Cytochrome c-like domain; 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:SF4; CYTOCHROME C-553; 1.
DR   PANTHER; PTHR34688; CYTOCHROME C6, CHLOROPLASTIC; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Photosynthesis; Thylakoid; Transport.
FT   CHAIN           1..87
FT                   /note="Cytochrome c6"
FT                   /id="PRO_0000208682"
FT   BINDING         14
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
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:0000250"
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:0000250"
SQ   SEQUENCE   87 AA;  9293 MW;  A69163A0582CD7E9 CRC64;
     ADTVSGAALF KANCAQCHVG GGNLVNRAKT LKKEALEKYN MYSAKAIIAQ VTHGKGAMPA
     FGIRLKAEQI ENVAAYVLEQ ADNGWKK
//