CYB6_SYNPW
ID CYB6_SYNPW Reviewed; 218 AA.
AC A5GJ44;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cytochrome b6 {ECO:0000255|HAMAP-Rule:MF_00633};
GN Name=petB {ECO:0000255|HAMAP-Rule:MF_00633};
GN OrderedLocusNames=SynWH7803_0533;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) 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:0000255|HAMAP-Rule:MF_00633}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_00633}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00633}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00633}.
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:0000255|HAMAP-Rule:MF_00633}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. PetB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00633}.
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DR EMBL; CT971583; CAK22959.1; -; Genomic_DNA.
DR RefSeq; WP_006042106.1; NC_009481.1.
DR AlphaFoldDB; A5GJ44; -.
DR SMR; A5GJ44; -.
DR STRING; 32051.SynWH7803_0533; -.
DR EnsemblBacteria; CAK22959; CAK22959; SynWH7803_0533.
DR KEGG; syx:SynWH7803_0533; -.
DR eggNOG; COG1290; Bacteria.
DR HOGENOM; CLU_031114_0_2_3; -.
DR OMA; WATQTGM; -.
DR OrthoDB; 1339825at2; -.
DR Proteomes; UP000001566; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived 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; 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; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..218
FT /note="Cytochrome b6"
FT /id="PRO_1000061416"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT BINDING 38
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT BINDING 89
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:0000255|HAMAP-Rule:MF_00633"
FT BINDING 103
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:0000255|HAMAP-Rule:MF_00633"
FT BINDING 190
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:0000255|HAMAP-Rule:MF_00633"
FT BINDING 205
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:0000255|HAMAP-Rule:MF_00633"
SQ SEQUENCE 218 AA; 24657 MW; 7BAF340921FC3BB7 CRC64;
MANSSPVYDW FQERLEIQDI ADDISSKYVP PHVNIFYCLG GITLVCFLIQ FATGFAMTFY
YKPTVAEAYS SVQYLMTDVS FGWLIRSVHR WSASMMVLML ILHVFRVYLT GGFKRPRELT
WVTGVTMAVI TVSFGVTGYS LPWDQVGYWA VKIVSGVPAA IPVVGDFMVE LLRGGESVGQ
STLTRFYSLH TFVMPWLLAV FMLMHFLMIR KQGISGPL
