CYC6_CHLRE
ID CYC6_CHLRE Reviewed; 148 AA.
AC P08197;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytochrome c6, chloroplastic;
DE AltName: Full=Cytochrome c-552 {ECO:0000303|PubMed:3036842};
DE AltName: Full=Cytochrome c-553;
DE AltName: Full=Cytochrome c553;
DE AltName: Full=Soluble cytochrome f;
DE Flags: Precursor;
GN Name=petJ;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=3036842; DOI=10.1016/s0021-9258(18)48047-7;
RA Merchant S., Bogorad L.;
RT "The Cu(II)-repressible plastidic cytochrome c. Cloning and sequence of a
RT complementary DNA for the pre-apoprotein.";
RL J. Biol. Chem. 262:9062-9067(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=1714451; DOI=10.1016/s0021-9258(18)98586-8;
RA Hill K.L., Li H.H., Singer J., Merchant S.;
RT "Isolation and structural characterization of the Chlamydomonas reinhardtii
RT gene for cytochrome c6. Analysis of the kinetics and metal specificity of
RT its copper-responsive expression.";
RL J. Biol. Chem. 266:15060-15067(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 59-148 IN COMPLEX WITH HEME,
RP COFACTOR, AND SUBUNIT.
RX PubMed=7623381; DOI=10.1006/jmbi.1995.0404;
RA Kerfeld C.A., Anwar H.P., Interrante R., Merchant S., Yeates T.O.;
RT "The structure of chloroplast cytochrome c6 at 1.9-A resolution: evidence
RT for functional oligomerization.";
RL J. Mol. Biol. 250:627-647(1995).
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: Thought to function as a monomer, however 2 crystal forms are
CC observed; a homodimer and homotrimer, suggesting the protein
CC oligomerizes. {ECO:0000269|PubMed:7623381}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000305}.
CC -!- INDUCTION: Induced in copper-deficient medium.
CC {ECO:0000269|PubMed:1714451, ECO:0000269|PubMed:3036842}.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC {ECO:0000269|PubMed:7623381}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.
CC {ECO:0000305}.
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DR EMBL; M67448; AAB00729.1; -; Genomic_DNA.
DR EMBL; J02774; AAA33081.1; -; mRNA.
DR PIR; A27113; CCKM6R.
DR RefSeq; XP_001698242.1; XM_001698190.1.
DR PDB; 1CYI; X-ray; 1.90 A; A=59-148.
DR PDB; 1CYJ; X-ray; 1.90 A; A=59-148.
DR PDBsum; 1CYI; -.
DR PDBsum; 1CYJ; -.
DR AlphaFoldDB; P08197; -.
DR SMR; P08197; -.
DR BioGRID; 983605; 1.
DR STRING; 3055.EDO99527; -.
DR EnsemblPlants; PNW71360; PNW71360; CHLRE_16g651050v5.
DR GeneID; 5723799; -.
DR Gramene; PNW71360; PNW71360; CHLRE_16g651050v5.
DR KEGG; cre:CHLRE_16g651050v5; -.
DR eggNOG; ENOG502SB4X; Eukaryota.
DR HOGENOM; CLU_101159_1_0_1; -.
DR OrthoDB; 1253356at2759; -.
DR EvolutionaryTrace; P08197; -.
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 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; Chloroplast; Electron transport; Heme; Iron; Metal-binding;
KW Photosynthesis; Plastid; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT CHAIN 59..148
FT /note="Cytochrome c6, chloroplastic"
FT /id="PRO_0000023850"
FT BINDING 72
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:7623381"
FT BINDING 75
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:7623381"
FT BINDING 76
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:0000269|PubMed:7623381"
FT BINDING 118
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:0000269|PubMed:7623381"
FT CONFLICT 107
FT /note="I -> S (in Ref. 1; AAA33081)"
FT /evidence="ECO:0000305"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:1CYI"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:1CYI"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1CYI"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1CYI"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:1CYI"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:1CYI"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1CYI"
FT HELIX 127..143
FT /evidence="ECO:0007829|PDB:1CYI"
SQ SEQUENCE 148 AA; 15427 MW; 091567E642F457E8 CRC64;
MLQLANRSVR AKAARASQSA RSVSCAAAKR GADVAPLTSA LAVTASILLT TGAASASAAD
LALGAQVFNG NCAACHMGGR NSVMPEKTLD KAALEQYLDG GFKVESIIYQ VENGKGAMPA
WADRLSEEEI QAVAEYVFKQ ATDAAWKY
