CYB_OENBE
ID CYB_OENBE Reviewed; 394 AA.
AC P09843;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 4.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cytochrome b;
DE AltName: Full=Complex III subunit 3;
DE AltName: Full=Complex III subunit III;
DE AltName: Full=Cytochrome b-c1 complex subunit 3;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
GN Name=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS Oenothera berteroana (Bertero's evening primrose).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX NCBI_TaxID=3950;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schuster W., Brennicke A.;
RT "TGA-Termination codon in the apocytochrome b gene from Oenothera
RT mitochondria.";
RL Curr. Genet. 9:157-163(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21, AND RNA EDITING.
RX PubMed=2326162; DOI=10.1093/nar/18.2.229;
RA Schuster W., Unseld M., Wissinger B., Brennicke A.;
RT "Ribosomal protein S14 transcripts are edited in Oenothera mitochondria.";
RL Nucleic Acids Res. 18:229-233(1990).
RN [3]
RP RNA EDITING.
RX PubMed=1725505; DOI=10.1007/bf00317068;
RA Schuster W., Ternes R., Knoop V., Hiesel R., Wissinger B., Brennicke A.;
RT "Distribution of RNA editing sites in Oenothera mitochondrial mRNAs and
RT rRNAs.";
RL Curr. Genet. 20:397-404(1991).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex) that is part of the
CC mitochondrial respiratory chain. The b-c1 complex mediates electron
CC transfer from ubiquinol to cytochrome c. Contributes to the generation
CC of a proton gradient across the mitochondrial membrane that is then
CC used for ATP synthesis. {ECO:0000250|UniProtKB:P00163}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P00163};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:P00163};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00163}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00163}.
CC -!- RNA EDITING: Modified_positions=19 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 97 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 101 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 104 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 110 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 121 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 137 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 190 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 286 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 304 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 329 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162}, 363 {ECO:0000269|PubMed:1725505,
CC ECO:0000269|PubMed:2326162};
CC -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at
CC about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs
CC at about 566 nm. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
CC -!- CAUTION: The protein contains only eight transmembrane helices, not
CC nine as predicted by bioinformatics tools.
CC {ECO:0000250|UniProtKB:P00163}.
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DR EMBL; X07126; CAA30135.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X17030; CAA34892.1; ALT_SEQ; Genomic_DNA.
DR PIR; S20141; CBOBE.
DR AlphaFoldDB; P09843; -.
DR SMR; P09843; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR CDD; cd00290; cytochrome_b_C; 1.
DR CDD; cd00284; Cytochrome_b_N; 1.
DR Gene3D; 1.20.810.10; -; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR030689; Cytochrome_b.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 1.
DR PIRSF; PIRSF038885; COB; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR SUPFAM; SSF81648; SSF81648; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Respiratory chain; RNA editing;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..394
FT /note="Cytochrome b"
FT /id="PRO_0000061314"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 83..105
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 355..374
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT BINDING 89
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b562"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT BINDING 103
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b566"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT BINDING 191
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b562"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT BINDING 204
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b566"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT BINDING 209
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
SQ SEQUENCE 394 AA; 44365 MW; 3ABF621E60ED9B11 CRC64;
MATIRNQRFS LLKQPISSIL NQHLIDYPTP SNLSYWWGFG SLAGICLVIQ IVTGVFLAMH
YTPHVDLAFN SVEHIMRDVE GGWLLRYMHA NGASMFFIVV YLHTFRGLYY ASYSSPREFV
WCLGVVIFLL MIVTAFIGYV LPWGQMSFWG ATVITSLASA IPVVGDTIVT WLWGGFSVDN
ATLNRFFSLY HLLPFILVGA SLLHLAALHQ YGSSNPLGVH SEMDKISFYP YFYVKDLVGW
VAFAIFFSIW IFYAPNVLGH PDNYIPANPM STPPHIVPEW YFLPIYAILR SIPDKAGGVA
AIALVFICLL ALPFFKDMYV RSSSFRPIYQ GIFWLLLADC LLLGWIGCQP VEAPFVTIGQ
ISSIVFFLFF AITPILGRVG RGIPNSYTDE TDHT
