ID A0A7S9HVX6_9APIA Unreviewed; 215 AA. AC A0A7S9HVX6; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 19-JAN-2022, entry version 3. DE RecName: Full=Cytochrome b6 {ECO:0000256|HAMAP-Rule:MF_00633}; GN Name=petB {ECO:0000256|HAMAP-Rule:MF_00633, GN ECO:0000313|EMBL:QPG24184.1}; OS Meeboldia delavayi. OG Plastid {ECO:0000313|EMBL:QPG24184.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Acronema clade; OC Meeboldia. OX NCBI_TaxID=165504 {ECO:0000313|EMBL:QPG24184.1}; RN [1] {ECO:0000313|EMBL:QPG24184.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=33182384; RA Gou W., Jia S.B., Price M., Guo X.L., Zhou S.D., He X.J.; RT "Complete Plastid Genome Sequencing of Eight Species from Hansenia, RT Haplosphaera and Sinodielsia (Apiaceae): Comparative Analyses and RT Phylogenetic Implications."; RL Plants (Basel) 9:0-E1523(2020). 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 -!- 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}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP- CC Rule:MF_00633}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00633}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass CC membrane protein {ECO:0000256|ARBA:ARBA00004141}. 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}. 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; MT843765; QPG24184.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-UniRule. 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; PTHR19271:SF20; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR SUPFAM; SSF81342; SSF81342; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00633}; KW Heme {ECO:0000256|HAMAP-Rule:MF_00633}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00633}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00633}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_00633}; Plastid {ECO:0000313|EMBL:QPG24184.1}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00633, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|HAMAP-Rule:MF_00633}. 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 183..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 METAL 86 FT /note="Iron (heme 2 axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" FT METAL 100 FT /note="Iron (heme 1 axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" FT METAL 187 FT /note="Iron (heme 2 axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" FT METAL 202 FT /note="Iron (heme 1 axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" FT BINDING 35 FT /note="Heme 1; covalent, via 1 link" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633" SQ SEQUENCE 215 AA; 24151 MW; 8D592BD517D4C72F CRC64; MSKVYDWFEE RLEIQAIADD ITSKYVPPHV NIFYCLGGIT LTCFLVQVAT GFAMTFYYRP TVTDAFASVQ YIMTEANFGW LIRSVHRWSA SMMVLMMILH VFRVYLTGGF KKPRELTWVT GVVLAVLTAS FGVTGYSLPR DQIGYWAVKI VTGVPEAIPV IGSPLVELLR GSTSVGQSTL TRFYSLHTFV LPLLTAVFML MHFPMIRKQG ISGPL //