CYC6_CLAGO
ID CYC6_CLAGO Reviewed; 91 AA.
AC P83391;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Cladophora glomerata.
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC Cladophorales; Cladophoraceae; Cladophora.
OX NCBI_TaxID=162068 {ECO:0000305};
RN [1]
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND X-RAY
RP CRYSTALLOGRAPHY (1.3 ANGSTROMS).
RX PubMed=12475218; DOI=10.1021/bi026473v;
RA Dikiy A., Carpentier W., Vandenberghe I.H.M., Borsari M., Safarov N.,
RA Dikaya E., Van Beeumen J., Ciurli S.;
RT "Structural basis for the molecular properties of cytochrome c6.";
RL Biochemistry 41:14689-14699(2002).
CC -!- FUNCTION: Functions as an electron carrier between membrane-bound
CC cytochrome b6-f and photosystem I in oxygenic photosynthesis.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 1LS9; X-ray; 1.30 A; A=1-91.
DR PDBsum; 1LS9; -.
DR AlphaFoldDB; P83391; -.
DR SMR; P83391; -.
DR EvolutionaryTrace; P83391; -.
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..91
FT /note="Cytochrome c6"
FT /id="PRO_0000208674"
FT BINDING 17
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 20
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 21
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 BINDING 63
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 HELIX 3..16
FT /evidence="ECO:0007829|PDB:1LS9"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:1LS9"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1LS9"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1LS9"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1LS9"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:1LS9"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1LS9"
FT HELIX 72..87
FT /evidence="ECO:0007829|PDB:1LS9"
SQ SEQUENCE 91 AA; 9833 MW; 2CAE8881CA8BD283 CRC64;
VDAELLADGK KVFAGNCAAC HLGGNNSVLA DKTLKKDAIE KYLEGGLTLE AIKYQVNNGK
GAMPAWADRL DEDDIEAVSN YVYDQAVNSK W