ID   C1PGE4_9LILI            Unreviewed;       306 AA.
AC   C1PGE4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Cytochrome f {ECO:0000256|ARBA:ARBA00013528};
DE   Flags: Fragment;
GN   Name=petA {ECO:0000313|EMBL:BAH57941.1};
OS   Potamogeton pusillus.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:BAH57941.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Potamogetonaceae; Potamogeton.
OX   NCBI_TaxID=246702 {ECO:0000313|EMBL:BAH57941.1};
RN   [1] {ECO:0000313|EMBL:BAH57941.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19247501; DOI=10.1371/journal.pone.0004633;
RA   Iida S., Miyagi A., Aoki S., Ito M., Kadono Y., Kosuge K.;
RT   "Molecular adaptation of rbcL in the heterophyllous aquatic plant
RT   Potamogeton.";
RL   PLoS ONE 4:e4633-e4633(2009).
CC   -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC       electron transfer between photosystem II (PSII) and photosystem I
CC       (PSI), cyclic electron flow around PSI, and state transitions.
CC       {ECO:0000256|ARBA:ARBA00003068}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602325-50};
CC       Note=Binds 1 heme group covalently. {ECO:0000256|PIRSR:PIRSR602325-50};
CC   -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC       cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and
CC       the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and
CC       PetN. The complex functions as a dimer.
CC       {ECO:0000256|ARBA:ARBA00025834}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family.
CC       {ECO:0000256|ARBA:ARBA00008923}.
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DR   EMBL; AB250142; BAH57941.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1PGE4; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; 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; 2.40.50.100; -; 1.
DR   Gene3D; 2.60.40.830; Cytochrome f large domain; 1.
DR   Gene3D; 1.20.5.700; Single helix bin; 1.
DR   HAMAP; MF_00610; Cytb6_f_cytF; 1.
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   PANTHER; PTHR33288; -; 1.
DR   PANTHER; PTHR33288:SF10; CYTOCHROME F; 1.
DR   Pfam; PF01333; Apocytochr_F_C; 1.
DR   Pfam; PF16639; Apocytochr_F_N; 1.
DR   PRINTS; PR00610; CYTOCHROMEF.
DR   SUPFAM; SSF103431; Cytochrome f subunit of the cytochrome b6f complex, transmembrane anchor; 1.
DR   SUPFAM; SSF49441; Cytochrome f, large domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS51010; CYTF; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:BAH57941.1};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602325-50};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602325-50};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602325-50};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Plastid {ECO:0000313|EMBL:BAH57941.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        286..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          36..190
FT                   /note="Cytochrome f large"
FT                   /evidence="ECO:0000259|Pfam:PF16639"
FT   BINDING         36
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:0000256|PIRSR:PIRSR602325-50"
FT   BINDING         56
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602325-50"
FT   BINDING         59
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602325-50"
FT   BINDING         60
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:0000256|PIRSR:PIRSR602325-50"
FT   NON_TER         306
FT                   /evidence="ECO:0000313|EMBL:BAH57941.1"
SQ   SEQUENCE   306 AA;  33580 MW;  BA1280D667D4D719 CRC64;
     MQNRNTFFVV REQITRSISV SIMIYIITHT SISNAYPIFA QQGYENPREA TGRIVCANCH
     LANKPVDIEV PQAVLPDTVF EAVVRIPYDR QVKQVLANGK KGGLNVGAVL ILPEGFELAP
     PDRISPEMKE KMGNLSFQSY RPTKKNILVI GPVPGQKYSE IVFPILSPDP TMKKDVHFLK
     YPIYVGGNRG RGQIYPDGSK SNNTVYNATS AGIVSKIVRK QKGGYEITIA DASDGHEVVD
     MIPPGPELLV SEGESIKLDQ PLTSNPNVGG FGQGDAEIVL QDPLRVQGLL FFFASIILAQ
     IFLVLK
//