ID   CYC6_CHLBR              Reviewed;          89 AA.
AC   Q09099;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Cytochrome c6;
DE   AltName: Full=Cytochrome c-552;
DE   AltName: Full=Cytochrome c-553;
DE   AltName: Full=Cytochrome c553;
DE   AltName: Full=Soluble cytochrome f;
GN   Name=petJ;
OS   Chlorolobion braunii (Green alga) (Monoraphidium braunii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Chlorolobion.
OX   NCBI_TaxID=34112;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8396033; DOI=10.1111/j.1432-1033.1993.tb18150.x;
RA   Campos A.P., Aguiar A.P., Hervas M., Regalla M., Navarro J.A., Ortega J.M.,
RA   Xavier A.V., de la Rosa M.A., Teixeira M.;
RT   "Cytochrome c6 from Monoraphidium braunii. A cytochrome with an unusual
RT   heme axial coordination.";
RL   Eur. J. Biochem. 216:329-341(1993).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
RX   PubMed=8591027; DOI=10.1016/s0969-2126(01)00252-0;
RA   Frazao C., Soares C.M., Carrondo M.A., Pohl E., Dauter Z., Wilson K.S.,
RA   Hervas M., Navarro J.A., de la Rosa M.A., Sheldrick G.M.;
RT   "Ab initio determination of the crystal structure of cytochrome c6 and
RT   comparison with plastocyanin.";
RL   Structure 3:1159-1169(1995).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=9538000; DOI=10.1021/bi972765y;
RA   Banci L., Bertini I., de la Rosa M.A., Koulougliotis D., Navarro J.A.,
RA   Walter O.;
RT   "Solution structure of oxidized cytochrome c6 from the green alga
RT   Monoraphidium braunii.";
RL   Biochemistry 37:4831-4843(1998).
CC   -!- FUNCTION: Functions as an electron carrier between membrane-bound
CC       cytochrome b6-f and photosystem I in oxygenic photosynthesis.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is +358 mV.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.
CC       {ECO:0000305}.
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DR   PIR; S35677; S35677.
DR   PDB; 1A2S; NMR; -; A=1-89.
DR   PDB; 1CED; NMR; -; A=1-89.
DR   PDB; 1CTJ; X-ray; 1.10 A; A=1-89.
DR   PDBsum; 1A2S; -.
DR   PDBsum; 1CED; -.
DR   PDBsum; 1CTJ; -.
DR   AlphaFoldDB; Q09099; -.
DR   SMR; Q09099; -.
DR   EvolutionaryTrace; Q09099; -.
DR   GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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-KW.
DR   Gene3D; 1.10.760.10; -; 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; Chloroplast; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Photosynthesis; Plastid; Thylakoid; Transport.
FT   CHAIN           1..89
FT                   /note="Cytochrome c6"
FT                   /id="PRO_0000208677"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:8396033"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:8396033"
FT   BINDING         19
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|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:8396033"
FT   BINDING         61
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|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:8396033"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:1CTJ"
FT   HELIX           16..19
FT                   /evidence="ECO:0007829|PDB:1CTJ"
FT   HELIX           20..22
FT                   /evidence="ECO:0007829|PDB:1CTJ"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:1CTJ"
FT   HELIX           34..40
FT                   /evidence="ECO:0007829|PDB:1CTJ"
FT   HELIX           47..56
FT                   /evidence="ECO:0007829|PDB:1CTJ"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:1A2S"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:1A2S"
FT   HELIX           70..85
FT                   /evidence="ECO:0007829|PDB:1CTJ"
SQ   SEQUENCE   89 AA;  9352 MW;  8625BD98FF88156D CRC64;
     EADLALGKAV FDGNCAACHA GGGNNVIPDH TLQKAAIEQF LDGGFNIEAI VYQIENGKGA
     MPAWDGRLDE DEIAGVAAYV YDQAAGNKW