ID C3VZR5_9SPER Unreviewed; 215 AA. AC C3VZR5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 29-MAY-2024, entry version 65. DE RecName: Full=Cytochrome b6 {ECO:0000256|ARBA:ARBA00035697, ECO:0000256|HAMAP-Rule:MF_00633}; GN Name=petB {ECO:0000256|HAMAP-Rule:MF_00633, GN ECO:0000313|EMBL:ACP51541.1}; GN ORFNames=PLC-449 {ECO:0000313|EMBL:ACP51541.1}; OS Pinus aristata. OG Plastid; Chloroplast {ECO:0000313|EMBL:ACP51541.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus; OC Pinus subgen. Strobus. OX NCBI_TaxID=71623 {ECO:0000313|EMBL:ACP51541.1}; RN [1] {ECO:0000313|EMBL:ACP51541.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ARIS02 {ECO:0000313|EMBL:ACP51541.1}; RX PubMed=19954512; DOI=10.1186/1741-7007-7-84; RA Parks M., Cronn R., Liston A.; RT "Increasing phylogenetic resolution at low taxonomic levels using massively RT parallel sequencing of chloroplast genomes."; RL BMC Biol. 7:84-84(2009). RN [2] {ECO:0000313|EMBL:ACP51541.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ARIS02 {ECO:0000313|EMBL:ACP51541.1}; RA Parks M.B., Liston A., Cronn R.C.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. 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 b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00633, CC ECO:0000256|RuleBase:RU003291}; CC Note=Binds 2 heme b groups non-covalently with two histidine residues CC as axial ligands. {ECO:0000256|HAMAP-Rule:MF_00633, CC ECO:0000256|RuleBase:RU003291}; CC -!- COFACTOR: CC Name=heme c; Xref=ChEBI:CHEBI:61717; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00633}; CC Note=Binds one heme group covalently by a single cysteine link with no CC axial amino acid ligand. This heme was named heme ci. CC {ECO:0000256|HAMAP-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; FJ899567; ACP51541.1; -; Genomic_DNA. DR AlphaFoldDB; C3VZR5; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:TreeGrafter. 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:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:TreeGrafter. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:TreeGrafter. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule. DR CDD; cd00284; Cytochrome_b_N; 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; IPR048259; Cytochrome_b_N_euk/bac. DR InterPro; IPR016174; Di-haem_cyt_TM. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF000032; Cytochrome_b6; 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:ACP51541.1}; 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:ACP51541.1}; 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 31..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..206 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 4..215 FT /note="Cytochrome b/b6 N-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51002" FT BINDING 35 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" FT BINDING 86 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" 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 b" FT /ligand_id="ChEBI:CHEBI:60344" 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 b" FT /ligand_id="ChEBI:CHEBI:60344" 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 b" FT /ligand_id="ChEBI:CHEBI:60344" 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; 24261 MW; E696F7DD72DB3DDD CRC64; MGKVYDWFEE RLEIQAIADD ITSKYVPPHV NIFYCLGGIT LTCFLVQVAT GFAMTFYYRP TVTEAFASVQ YLMTEVNFGW LIRSIHRWSA SMMVLMMILH VFRVYLTGGF KKPRELTWVT GVILAVLTVS FGVTGYSLPW DQIGYWAVKI VTGVPEAIPV IGSPLVELLR GSVSVGQSTL TRFYSLHTFI LPLLTAVFMP MHFLMIRKQG ISGPL //