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CYB6_CUSGR
ID   CYB6_CUSGR              Reviewed;         218 AA.
AC   A7M927;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Cytochrome b6;
GN   Name=petB;
OS   Cuscuta gronovii (Common dodder) (Epithymum gronovii).
OG   Plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC   Cuscuta subgen. Grammica; Cuscuta sect. Oxycarpae.
OX   NCBI_TaxID=35886;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ABSENCE OF RNA EDITING.
RX   PubMed=17714582; DOI=10.1186/1471-2229-7-45;
RA   Funk H.T., Berg S., Krupinska K., Maier U.-G., Krause K.;
RT   "Complete DNA sequences of the plastid genomes of two parasitic flowering
RT   plant species, Cuscuta reflexa and Cuscuta gronovii.";
RL   BMC Plant Biol. 7:45-45(2007).
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:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 2 heme groups. One heme group is bound covalently by a
CC       single cysteine link, the other one non-covalently. {ECO:0000250};
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid thylakoid membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family. PetB subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC       some thylakoids, although the photosynthetic activity does not exceed
CC       the light compensation point. {ECO:0000305}.
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DR   EMBL; AM711639; CAM98355.1; -; Genomic_DNA.
DR   RefSeq; YP_001430068.1; NC_009765.1.
DR   AlphaFoldDB; A7M927; -.
DR   SMR; A7M927; -.
DR   PRIDE; A7M927; -.
DR   GeneID; 5536724; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055035; C:plastid 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   2: Evidence at transcript level;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW   Plastid; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..218
FT                   /note="Cytochrome b6"
FT                   /id="PRO_0000308480"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         38
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
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:0000250"
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:0000250"
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:0000250"
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:0000250"
SQ   SEQUENCE   218 AA;  24665 MW;  FE2B3A6371BF1703 CRC64;
     MSNVNKVYDW FEERLEIQAI ADDITSKYVP PHVNIFYCLG GITLTCFLVQ VATGFAMTFY
     YRPIVNEAFA SVQYIMIEAN FGWLIRSVHR WSASMMVLMM ILHVFRVYLT GGFKKPRELT
     WVTGVLLGVL TASFGVTGYS LPWDQTGYWA IKIVTGVPEA IPLIGAPMVE LLRGSASVGQ
     FTLTRFYSLH TFVLPLITIV FMLMHFLMIR KQGISGPL
 
 
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