CYB_WHEAT
ID CYB_WHEAT Reviewed; 398 AA.
AC P07747;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 125.
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 Triticum aestivum (Wheat).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2987849; DOI=10.1093/nar/13.7.2281;
RA Boer P.H., McIntosh J.E., Gray M.W., Bonen L.;
RT "The wheat mitochondrial gene for apocytochrome b: absence of a prokaryotic
RT ribosome binding site.";
RL Nucleic Acids Res. 13:2281-2292(1985).
RN [2]
RP RNA EDITING.
RX PubMed=2552325; DOI=10.1038/341660a0;
RA Gualberto J.M., Lamattina L., Bonnard G., Weil J.-H., Grienenberger J.-M.;
RT "RNA editing in wheat mitochondria results in the conservation of protein
RT sequences.";
RL Nature 341:660-662(1989).
RN [3]
RP RNA EDITING.
RX PubMed=7504589; DOI=10.1007/bf00336787;
RA Zanlungo S., Begu D., Quinones V., Araya A., Jordana X.;
RT "RNA editing of apocytochrome b (cob) transcripts in mitochondria from two
RT genera of plants.";
RL Curr. Genet. 24:344-348(1993).
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=60 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 96 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 100 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 109 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 120 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 140 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 190 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 194 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 227 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 239 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 242 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 270 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 285 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 303 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 328 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 361 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589}, 375 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:7504589};
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; X02352; CAA26207.1; ALT_SEQ; Genomic_DNA.
DR PIR; A22931; A22931.
DR RefSeq; YP_398402.1; NC_007579.1.
DR AlphaFoldDB; P07747; -.
DR SMR; P07747; -.
DR STRING; 4565.EPlTAEP00000010083; -.
DR eggNOG; KOG4663; Eukaryota.
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..398
FT /note="Cytochrome b"
FT /id="PRO_0000061724"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 82..104
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT BINDING 88
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 102
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 189
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 203
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 208
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
SQ SEQUENCE 398 AA; 45103 MW; 183F0741D5ECD42A CRC64;
MTIRNQRFSL LKQPIYSTLN QHLIDYPTPS NLSYWWGFGS LAGICLVIQI VTGVFLAMHY
TPHVDLAFNS VEHIMRDVEG GWLLRYMHAN GASMFFIVVY LHIFRGLYYA SYSSPREFVW
CLGVVIFLLM IVTAFIGYVL PWGQMSFWGA TVITSLASAI PVVGDTIVTW LWGGFSVDNA
TLNRFFSLHY LLPFILVGAS LLHLAALHQY GSNNPLGVHS EMDKIAFYPY FYVKDLVGWV
AFAIFFSIWI FFAPNVLGHP DNYIPANPMS TPPHIVPEWY FLPIYAILRS IPDKAGGVAA
IALVFISLLA LPFFKEMYVR SSSFRPIYQG IFWLLLADCL LLGWIGCQPV EAPFVTIGQI
SSVFFFLFFA ITPILGRVGR GIPKYYTDET HRTGSFWP
