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CYB6_HELGE
ID   CYB6_HELGE              Reviewed;         213 AA.
AC   Q9L598;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Cytochrome b6 {ECO:0000255|HAMAP-Rule:MF_00633};
GN   Name=petB {ECO:0000255|HAMAP-Rule:MF_00633};
GN   Synonyms=cytB {ECO:0000255|HAMAP-Rule:MF_00633};
OS   Heliomicrobium gestii (Heliobacterium gestii).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliomicrobium.
OX   NCBI_TaxID=2699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43375 / DSM 11169 / Chainat;
RA   Albert I.;
RT   "Gene cluster coding for redox proteins of a putative cytochrome bc complex
RT   in Heliobacterium gestii.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the cytochrome bc complex which donates
CC       electrons to the photosynthetic reaction center. {ECO:0000255|HAMAP-
CC       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 subunits of the cytochrome bc complex are a Rieske Fe-S
CC       protein (PetC), cytochrome b6 (PetB), subunit IV (PetD), and a diheme
CC       cytochrome c (PetX). {ECO:0000255|HAMAP-Rule:MF_00633}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00633};
CC       Multi-pass membrane protein {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; AF254191; AAF68086.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L598; -.
DR   SMR; Q9L598; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma 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   Pfam; PF00033; Cytochrome_B; 1.
DR   SUPFAM; SSF81342; SSF81342; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Photosynthesis; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..213
FT                   /note="Cytochrome b6"
FT                   /id="PRO_0000061839"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   BINDING         33
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         84
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         98
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         185
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         200
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   213 AA;  24004 MW;  39B92AE67D133DD3 CRC64;
     MKWLEERFPG IGHVAKDVAD HPVPSHTLNI FFCLGGLTLL CFIVQCLTGI FLAFYYKPTP
     EAAFTSVQMI TNEVRFGSVI RSMHHWSCQL MILLVFLHML RVYYTGAFKR PRELNWVAGC
     FLLVLSLALA FTGYLLPYEQ LSYWASVIGA ETANTLPVVG PTLKIMMQGG IKVTAEMLSR
     FYVLHVMILP AVAIIFLVAH FIMIRVQGIS DPM
 
 
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