ID A0A2S1CEH5_PEA Unreviewed; 215 AA. AC A0A2S1CEH5; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 14-DEC-2022, entry version 18. DE RecName: Full=Cytochrome b6 {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|RuleBase:RU003291}; GN Name=petB {ECO:0000256|HAMAP-Rule:MF_00633, GN ECO:0000313|EMBL:AWD26711.1}; OS Pisum sativum subsp. elatius. OG Plastid; Chloroplast {ECO:0000313|EMBL:AWD26711.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum. OX NCBI_TaxID=47742 {ECO:0000313|EMBL:AWD26711.1}; RN [1] {ECO:0000313|EMBL:AXY95583.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IG64350 {ECO:0000313|EMBL:AXY95879.1}, JI3233 RC {ECO:0000313|EMBL:AXY95657.1}, JI3557 {ECO:0000313|EMBL:AXY95583.1}, RC PI344537 {ECO:0000313|EMBL:AXY95953.1}, Pis2853 RC {ECO:0000313|EMBL:AXY95805.1}, and W6_26109 RC {ECO:0000313|EMBL:AXY95731.1}; RX PubMed=30195476; DOI=10.1016/j.ympev.2018.09.002; RA Bogdanova V.S., Mglinets A.V., Shatskaya N.V., Kosterin O.E., RA Solovyev V.I., Vasiliev G.V.; RT "Cryptic divergences in the genus Pisum L. (peas), as revealed by RT phylogenetic analysis of plastid genomes."; RL Mol. Phylogenet. Evol. 129:280-290(2018). RN [2] {ECO:0000313|EMBL:AWD26711.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CE1 {ECO:0000313|EMBL:AWD26785.1}, JI1091 RC {ECO:0000313|EMBL:AWD26637.1}, and JI1096 RC {ECO:0000313|EMBL:AWD26711.1}; RA Bogdanova V.S., Mglinets A.V., Shatskaya N.V., Kosterin O.E., RA Vasiliev G.V.; RT "Cryptic divergences in the genus Pisum L., as revealed by comparative RT analysis of complete plastid genomes."; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:QTC07652.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=33684529; RA Bogdanova V.S., Shatskaya N.V., Mglinets A.V., Kosterin O.E., RA Vasiliev G.V.; RT "Discordant evolution of organellar genomes in peas (Pisum L.)."; RL Mol. Phylogenet. Evol. 107136:0-0(2021). 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, ECO:0000256|HAMAP-Rule:MF_00633, CC ECO:0000256|RuleBase:RU003291}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00633}; CC Note=Binds 2 heme groups. One heme group is bound covalently by a CC single cysteine link, the other one non-covalently. {ECO:0000256|HAMAP- CC Rule:MF_00633}; 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. {ECO:0000256|ARBA:ARBA00025834, CC ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|RuleBase:RU003291}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_00633, CC ECO:0000256|RuleBase:RU003291}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|RuleBase:RU003291}. CC -!- MISCELLANEOUS: Heme 1 (or BH or b566) is high-potential and absorbs at CC about 566 nm, and heme 2 (or BL or b562) is low-potential and absorbs CC at about 562 nm. {ECO:0000256|HAMAP-Rule:MF_00633}. CC -!- SIMILARITY: Belongs to the cytochrome b family. PetB subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|RuleBase:RU003291}. 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 EMBL; MG859920; AWD26637.1; -; Genomic_DNA. DR EMBL; MG859921; AWD26711.1; -; Genomic_DNA. DR EMBL; MG859922; AWD26785.1; -; Genomic_DNA. DR EMBL; MG833029; AXK15387.1; -; Genomic_DNA. DR EMBL; MG882484; AXY95583.1; -; Genomic_DNA. DR EMBL; MG882485; AXY95657.1; -; Genomic_DNA. DR EMBL; MG882486; AXY95731.1; -; Genomic_DNA. DR EMBL; MG882487; AXY95805.1; -; Genomic_DNA. DR EMBL; MG882488; AXY95879.1; -; Genomic_DNA. DR EMBL; MG882489; AXY95953.1; -; Genomic_DNA. DR EMBL; MW181849; QTC07652.1; -; Genomic_DNA. DR EMBL; MW181850; QTC07726.1; -; Genomic_DNA. DR EMBL; MW181851; QTC07800.1; -; Genomic_DNA. DR EMBL; MW181853; QTC07948.1; -; Genomic_DNA. DR EMBL; MW192445; QTC08022.1; -; Genomic_DNA. DR EMBL; MW192446; QTC08096.1; -; Genomic_DNA. DR EMBL; MW286210; QTC30992.1; -; Genomic_DNA. DR EMBL; MW286211; QTC31066.1; -; Genomic_DNA. DR EMBL; MW286212; QTC31140.1; -; Genomic_DNA. DR EMBL; MW292563; QTC31288.1; -; Genomic_DNA. DR EMBL; MW292564; QTC31362.1; -; Genomic_DNA. DR EMBL; MW308610; QTC31436.1; -; Genomic_DNA. DR EMBL; MW308611; QTC31510.1; -; Genomic_DNA. DR EMBL; MW363526; QTC31584.1; -; Genomic_DNA. DR EMBL; MW363527; QTC31658.1; -; Genomic_DNA. DR EMBL; MW363528; QTC31732.1; -; Genomic_DNA. DR EMBL; MW363529; QTC31806.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2S1CEH5; -. DR SMR; A0A2S1CEH5; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR CDD; cd00284; Cytochrome_b_N; 1. DR Gene3D; 1.20.810.10; -; 1. DR HAMAP; MF_00633; Cytb6_f_cytb6; 1. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR023530; Cyt_B6_PetB. DR InterPro; IPR027387; Cytb/b6-like_sf. DR InterPro; IPR016174; Di-haem_cyt_TM. DR PANTHER; PTHR19271:SF20; -; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|RuleBase:RU003291, ECO:0000313|EMBL:AWD26711.1}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00633, KW ECO:0000256|RuleBase:RU003291}; KW Heme {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|RuleBase:RU003291}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|RuleBase:RU003291}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00633, KW ECO:0000256|RuleBase:RU003291}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_00633}; Plastid {ECO:0000313|EMBL:AWD26711.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|RuleBase:RU003291}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00633, KW ECO:0000256|RuleBase:RU003291}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00633, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|RuleBase:RU003291}. FT TRANSMEM 32..58 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 88..106 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 118..138 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 184..203 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 4..215 FT /note="CYTB_NTER" FT /evidence="ECO:0000259|PROSITE:PS51002" FT BINDING 35 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" FT BINDING 86 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" FT BINDING 100 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" FT BINDING 187 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" FT BINDING 202 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" SQ SEQUENCE 215 AA; 24112 MW; 1F438D73D5E460FC CRC64; MSKVYDWFEE RLEIQAIADD ITSKYVPPHV NIFYCLGGIT LTCFLVQVAT GFAMTFYYRP TVTEAFASVQ YIMTEANFGW LIRSVHRWSA SMMVLMMILH VFRVYLTGGF KKPRELTWVT GVVLGVLTAS FGVTGYSLPW DQIGYWAVKI VTGVPDAIPV IGSSVVELLR GSASVGQSTL TRFYSLHTFV LPLLTAVFML MHFPMIRKQG ISGPL //