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CYB6_PROHO
ID   CYB6_PROHO              Reviewed;         222 AA.
AC   P28058;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cytochrome b6 {ECO:0000255|HAMAP-Rule:MF_00633};
GN   Name=petB {ECO:0000255|HAMAP-Rule:MF_00633};
OS   Prochlorothrix hollandica.
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Prochlorotrichaceae;
OC   Prochlorothrix.
OX   NCBI_TaxID=1223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1623188; DOI=10.1007/bf00023383;
RA   Greer K.L., Golden S.S.;
RT   "Conserved relationship between psbH and petBD genes: presence of a shared
RT   upstream element in Prochlorothrix hollandica.";
RL   Plant Mol. Biol. 19:355-365(1992).
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; X60313; CAA42859.1; -; Genomic_DNA.
DR   PIR; S22470; S22470.
DR   AlphaFoldDB; P28058; -.
DR   SMR; P28058; -.
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   Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..222
FT                   /note="Cytochrome b6"
FT                   /id="PRO_0000061829"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   BINDING         42
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         93
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         107
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         194
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         209
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   222 AA;  25195 MW;  B605F74C32253633 CRC64;
     MFTKQVQESG VYKWFNDRLE IEAISDDISS KYVPPHVNIF YCLGGITLVC FIIQFATGFA
     MTFYYKPSVT EAFTSVQYLM NEVSFGWLIR SIHRWSASMM VLMMILHVFR VYLTGGFKNP
     RELTWITGVI LAVITVSFGV TGYSLPWDQV GYWAVKIVSG VPEAIPLVGP LMVELIRGSA
     SVGQATLTRF YSLHTFVLPW FIAVFMLMHF LMIRKQGISG PL
 
 
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