CYB6_DAUCA
ID CYB6_DAUCA Reviewed; 215 AA.
AC Q0G9T2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cytochrome b6 {ECO:0000255|HAMAP-Rule:MF_00633};
GN Name=petB {ECO:0000255|HAMAP-Rule:MF_00633};
OS Daucus carota (Wild carrot).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=4039;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Danvers Half-long;
RX PubMed=16945140; DOI=10.1186/1471-2164-7-222;
RA Ruhlman T., Lee S.-B., Jansen R.K., Hostetler J.B., Tallon L.J., Town C.D.,
RA Daniell H.;
RT "Complete plastid genome sequence of Daucus carota: implications for
RT biotechnology and phylogeny of angiosperms.";
RL BMC Genomics 7:222-222(2006).
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: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00633}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-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; DQ898156; ABI32453.1; -; Genomic_DNA.
DR RefSeq; YP_740147.1; NC_008325.1.
DR AlphaFoldDB; Q0G9T2; -.
DR SMR; Q0G9T2; -.
DR EnsemblPlants; KZM81253; KZM81253; DCAR_032515.
DR GeneID; 4266774; -.
DR Gramene; KZM81253; KZM81253; DCAR_032515.
DR OMA; RWSAHAM; -.
DR OrthoDB; 1125966at2759; -.
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-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 Chloroplast; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Photosynthesis; Plastid; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..215
FT /note="Cytochrome b6"
FT /id="PRO_0000275313"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT BINDING 35
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 86
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 100
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 187
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 202
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 215 AA; 24121 MW; 8D593AD517C5C72F CRC64;
MSKVYDWFEE RLEIQAIADD ITSKYVPPHV NIFYCLGGIT LTCFLVQVAT GFAMTFYYRP
TVTDAFASVQ YIMTEANFGW LIRSVHRWSA SMMVLMMILH VFRVYLTGGF KKPRELTWVT
GVVLAVLTAS FGVTGYSLPR DQIGYWAVKI VTGVPEAIPV IGSPLVELLR GSASVGQSTL
TRFYSLHTFV LPLLTAVFML MHFPMIRKQG ISGPL
