ID   CYF_EUGGR               Reviewed;         496 AA.
AC   Q8GZR2;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Cytochrome f, chloroplastic;
DE   Flags: Precursor;
GN   Name=petA;
OS   Euglena gracilis.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3039 {ECO:0000312|EMBL:AAO13958.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 150-174, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=12837550; DOI=10.1016/s0005-2728(03)00058-6;
RA   Santillan Torres J.L., Atteia A., Claros M.G., Gonzalez-Halphen D.;
RT   "Cytochrome f and subunit IV, two essential components of the
RT   photosynthetic bf complex typically encoded in the chloroplast genome, are
RT   nucleus-encoded in Euglena gracilis.";
RL   Biochim. Biophys. Acta 1604:180-189(2003).
CC   -!- FUNCTION: Translocates protons across the thylakoid membrane and
CC       transfers electrons from photosystem II to photosystem I. It receives
CC       electrons from the Rieske iron-sulfur protein and passes them to
CC       plastocyanin. {ECO:0000250|UniProtKB:P23577}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 heme group covalently. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with plastocyanin and Rieske iron-sulfur protein.
CC       {ECO:0000250|UniProtKB:P23577}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:12837550}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:12837550}.
CC   -!- MISCELLANEOUS: This polypeptide is nuclear encoded in Euglena gracilis,
CC       but is chloroplast encoded in other plant species.
CC       {ECO:0000269|PubMed:12837550}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO13958.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF443625; AAO13958.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q8GZR2; -.
DR   SMR; Q8GZR2; -.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031361; C:integral component of thylakoid membrane; IEA:InterPro.
DR   GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
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; 2.60.40.830; -; 2.
DR   InterPro; IPR024058; Cyt-f_TM.
DR   InterPro; IPR002325; Cyt_f.
DR   InterPro; IPR024094; Cyt_f_lg_dom.
DR   InterPro; IPR036826; Cyt_f_lg_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF01333; Apocytochr_F_C; 1.
DR   Pfam; PF16639; Apocytochr_F_N; 2.
DR   PRINTS; PR00610; CYTOCHROMEF.
DR   SUPFAM; SSF103431; SSF103431; 1.
DR   SUPFAM; SSF49441; SSF49441; 2.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   PROSITE; PS51010; CYTF; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Membrane; Metal-binding; Photosynthesis; Photosystem I; Photosystem II;
KW   Plastid; Thylakoid; Transit peptide; Transmembrane; Transmembrane helix;
KW   Transport.
FT   TRANSIT         1..149
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:12837550"
FT   CHAIN           150..496
FT                   /note="Cytochrome f, chloroplastic"
FT                   /id="PRO_0000023841"
FT   TRANSMEM        462..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         150
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   496 AA;  52366 MW;  171A3B1FF1DD8087 CRC64;
     MASLQTPVMV GTVVGCVAGV VGFLAMSSNA ATSLSVAPAS TSTQIIANPS VIAPQYQGSV
     TSEDVAMEAS QTDFAEVAEI SSPVQVQSWS MIFSAMLAVP LAAAAMFFMK KSTTEERRPL
     VSIDDLLSVG KKAVVASAVV GAAAGSANAY PIFAQQAYGN PREATGRIVC ANCHLASKPT
     EIEVPQAVLP DQVFEAVTKV PFSGPSGFFN VVDPSTVVGS VTFAGTQPVG FIQESGVPVS
     QALVDIATPG TPDTVFKATI KVPYDESLKQ VAGNGRAAPL NVGAVLILPE GFRLAPPERI
     PEKMKEEING LQFIQYSKDT PNILVVGPVP GKKYAEMTVA LLSPDPRVDK KAEFGTLPIY
     VGGNRGRGQL YPTGEKSNNN IYNVEHSGKI ADIQLNEKKR IYTVAVQQKD GEIINEDLPA
     GAELIVKVGD VVEAGQAIST NPNVGGFGQA ESEIVLQNPG RVQAFLFFSF TVLATQTLLV
     VKKKQYEQVQ LSEMNF