CYC6_MICAE
ID CYC6_MICAE Reviewed; 81 AA.
AC P00112;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 109.
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 Microcystis aeruginosa.
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=1126;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2539045; DOI=10.1016/0003-9861(89)90023-4;
RA Cohn C.L., Hermodson M.A., Krogmann D.W.;
RT "The amino acid sequence of cytochrome c553 from Microcystis aeruginosa.";
RL Arch. Biochem. Biophys. 270:219-226(1989).
RN [2]
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; A00104; CCIA6.
DR PIR; S03859; S03859.
DR AlphaFoldDB; P00112; -.
DR SMR; P00112; -.
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 Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Photosynthesis; Thylakoid; Transport.
FT CHAIN 1..81
FT /note="Cytochrome c6"
FT /id="PRO_0000208683"
FT BINDING 10
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 14
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 54
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 CONFLICT 34..35
FT /note="KY -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="M -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 81 AA; 8421 MW; 8BF129DD7B0FFB09 CRC64;
DGASIFSANC ASCHMGGKNV VNAAKTLKKE DLVKYGKDSV EAIVTQVTKG MGAMPAFGGR
LSAEDIEAVA NYVLAQAEKG W