CYB6_TRIEI
ID CYB6_TRIEI Reviewed; 222 AA.
AC Q116S5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome b6 {ECO:0000255|HAMAP-Rule:MF_00633};
GN Name=petB {ECO:0000255|HAMAP-Rule:MF_00633}; OrderedLocusNames=Tery_1137;
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-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; CP000393; ABG50499.1; -; Genomic_DNA.
DR RefSeq; WP_011610885.1; NC_008312.1.
DR AlphaFoldDB; Q116S5; -.
DR SMR; Q116S5; -.
DR STRING; 203124.Tery_1137; -.
DR EnsemblBacteria; ABG50499; ABG50499; Tery_1137.
DR KEGG; ter:Tery_1137; -.
DR eggNOG; COG1290; Bacteria.
DR HOGENOM; CLU_031114_0_2_3; -.
DR OMA; WATQTGM; -.
DR OrthoDB; 1339825at2; -.
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_1000082638"
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; 25186 MW; 556D1BBEDD55B922 CRC64;
MFSKQVTDSP AYKWFDERLE VQALADDISS KYVPPHVNIF YCLGGITLVC FLIQFATGFA
MTFYYKPTVT EALASVQYIM TEVNFGWLIR SIHRWSASMM VLMMILHTFR VYLTGGFKKP
RELTWVTGVV MAVITVSFGV TGYSLPWDQI GYWAVKIVSG VPDAIPFVGP FIVELMRGST
SVGQATLTRF YSLHTFVLPW FIAVFMLLHF LMIRKQGISG PL
