CYB6_NOSS1
ID CYB6_NOSS1 Reviewed; 215 AA.
AC P0A384; Q9L3Q1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cytochrome b6 {ECO:0000255|HAMAP-Rule:MF_00633};
GN Name=petB {ECO:0000255|HAMAP-Rule:MF_00633}; OrderedLocusNames=alr3421;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Arnold M.;
RT "b6f complex of Anabaena sp.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; AJ319645; CAC39602.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB75120.1; -; Genomic_DNA.
DR PIR; AF2233; AF2233.
DR RefSeq; WP_010997571.1; NZ_RSCN01000015.1.
DR PDB; 2ZT9; X-ray; 3.00 A; A=1-215.
DR PDB; 4H44; X-ray; 2.70 A; A=1-215.
DR PDB; 4OGQ; X-ray; 2.50 A; A=1-215.
DR PDBsum; 2ZT9; -.
DR PDBsum; 4H44; -.
DR PDBsum; 4OGQ; -.
DR AlphaFoldDB; P0A384; -.
DR SMR; P0A384; -.
DR DIP; DIP-61000N; -.
DR IntAct; P0A384; 7.
DR STRING; 103690.17132554; -.
DR TCDB; 3.D.3.5.6; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR PRIDE; P0A384; -.
DR EnsemblBacteria; BAB75120; BAB75120; BAB75120.
DR GeneID; 58726228; -.
DR KEGG; ana:alr3421; -.
DR eggNOG; COG1290; Bacteria.
DR OMA; WATQTGM; -.
DR OrthoDB; 1339825at2; -.
DR EvolutionaryTrace; P0A384; -.
DR Proteomes; UP000002483; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Photosynthesis; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..215
FT /note="Cytochrome b6"
FT /id="PRO_0000061824"
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"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:4OGQ"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:4OGQ"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 79..106
FT /evidence="ECO:0007829|PDB:4OGQ"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2ZT9"
FT HELIX 115..136
FT /evidence="ECO:0007829|PDB:4OGQ"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:4OGQ"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:4OGQ"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:4OGQ"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:4OGQ"
FT HELIX 190..209
FT /evidence="ECO:0007829|PDB:4OGQ"
SQ SEQUENCE 215 AA; 24273 MW; 272ECF1C60C4A963 CRC64;
MANVYDWFEE RLEIQAIAED VTSKYVPPHV NIFYCLGGIT LVCFLIQFAT GFAMTFYYKP
TVAEAYSSVQ YIMNEVNFGW LIRSIHRWSA SMMVLMMILH VFRVYLTGGF KKPRELTWVS
GVILAVITVS FGVTGYSLPW DQVGYWAVKI VSGVPEAIPV VGVLISDLLR GGSSVGQATL
TRYYSAHTFV LPWLIAVFML FHFLMIRKQG ISGPL
