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-OCT-2014, entry version 33. DE RecName: Full=Cytochrome b6 {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; Pinidae; Pinales; Pinaceae; Pinus; 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 RT massively 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|HAMAP-Rule:MF_00633}. CC -!- COFACTOR: Binds 2 heme groups. One heme group is bound covalently CC by a single cysteine link, the other one non-covalently. 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 CC and the Rieske protein, while the 4 small subunits are PetG, PetL, CC PetM and PetN. The complex functions as a dimer. CC {ECO:0000256|HAMAP-Rule:MF_00633}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_00633}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_00633}. CC -!- MISCELLANEOUS: Heme 1 (or BH or b566) is high-potential and CC absorbs at about 566 nm, and heme 2 (or BL or b562) is low- CC potential and absorbs at about 562 nm. {ECO:0000256|HAMAP- CC 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; FJ899567; ACP51541.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:UniProtKB-HAMAP. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-HAMAP. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. 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. DR InterPro; IPR016174; Di-haem_cyt_TM. DR Pfam; PF13631; Cytochrom_B_N_2; 1. DR PIRSF; PIRSF000032; Cytochrome_b6; 1. DR SUPFAM; SSF81342; SSF81342; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:ACP51541.1}; 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}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00633}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00633}; KW Plastid {ECO:0000313|EMBL:ACP51541.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00633}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00633}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00633}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00633}. FT TRANSMEM 32 52 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00633}. FT TRANSMEM 90 110 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00633}. FT TRANSMEM 116 136 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00633}. FT TRANSMEM 186 206 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00633}. FT METAL 86 86 Iron (heme 2 axial ligand). FT {ECO:0000256|HAMAP-Rule:MF_00633}. FT METAL 100 100 Iron (heme 1 axial ligand). FT {ECO:0000256|HAMAP-Rule:MF_00633}. FT METAL 187 187 Iron (heme 2 axial ligand). FT {ECO:0000256|HAMAP-Rule:MF_00633}. FT METAL 202 202 Iron (heme 1 axial ligand). FT {ECO:0000256|HAMAP-Rule:MF_00633}. FT BINDING 35 35 Heme 1 (covalent; via 1 link). FT {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 //