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Cytochrome b (Complex III subunit 3) (Complex III subunit CYTB) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Cytochrome b-c1 complex subunit CYTB) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit)

 CYB_YEAST               Reviewed;         385 AA.
P00163; A0A0A7NYK0; Q35802; Q35807; Q36301; Q9ZZW9;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-APR-2003, sequence version 3.
18-JUL-2018, entry version 166.
RecName: Full=Cytochrome b;
AltName: Full=Complex III subunit 3;
AltName: Full=Complex III subunit CYTB;
AltName: Full=Complex III subunit III;
AltName: Full=Cytochrome b-c1 complex subunit 3;
AltName: Full=Cytochrome b-c1 complex subunit CYTB;
AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
Name=COB; Synonyms=CYTB; OrderedLocusNames=Q0105;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Mitochondrion.
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=D273-10B/A21;
PubMed=6253454;
Nobrega F.G., Tzagoloff A.;
"Assembly of the mitochondrial membrane system. DNA sequence and
organization of the cytochrome b gene in Saccharomyces cerevisiae
D273-10B.";
J. Biol. Chem. 255:9828-9837(1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=D273-10B/A21;
PubMed=6383504;
Bonjardim C.A., Nobrega F.G.;
"Revision of the nucleotide sequence at the last intron of the
mitochondrial apocytochrome b gene in Saccharomyces cerevisiae.";
Braz. J. Med. Biol. Res. 17:17-20(1984).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=WR200;
PubMed=7737175; DOI=10.1111/j.1432-1033.1995.0762m.x;
Claros M.G., Perea J., Shu Y., Samatey F.A., Popot J.-L., Jacq C.;
"Limitations to in vivo import of hydrophobic proteins into yeast
mitochondria. The case of a cytoplasmically synthesized apocytochrome
b.";
Eur. J. Biochem. 228:762-771(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9872396; DOI=10.1016/S0014-5793(98)01467-7;
Foury F., Roganti T., Lecrenier N., Purnelle B.;
"The complete sequence of the mitochondrial genome of Saccharomyces
cerevisiae.";
FEBS Lett. 440:325-331(1998).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-143.
STRAIN=ATCC 44821 / 777-3A;
PubMed=7004642; DOI=10.1016/0092-8674(80)90344-X;
Lazowska J., Jacq C., Slonimski P.P.;
"Sequence of introns and flanking exons in wild-type and box3 mutants
of cytochrome b reveals an interlaced splicing protein coded by an
intron.";
Cell 22:333-348(1980).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-169.
STRAIN=ATCC 44821 / 777-3A;
PubMed=7034963; DOI=10.1016/0092-8674(81)90355-X;
Lazowska J., Jacq C., Slonimski P.P.;
"Splice points of the third intron in the yeast mitochondrial
cytochrome b gene.";
Cell 27:12-14(1981).
[8]
MUTANT W7, AND FUNCTION.
PubMed=2551731; DOI=10.1016/0014-5793(89)81050-6;
Brivet-Chevillotte P., di Rago J.-P.;
"Electron-transfer restoration by vitamin K3 in a complex III-
deficient mutant of S. cerevisiae and sequence of the corresponding
cytochrome b mutation.";
FEBS Lett. 255:5-9(1989).
[9]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND PROTEIN SEQUENCE OF
66-76.
PubMed=8031140; DOI=10.1006/abbi.1994.1312;
Beattie D.S., Jenkins H.C., Howton M.M.;
"Biochemical evidence for the orientation of cytochrome b in the yeast
mitochondrial membrane in the eight-helix model.";
Arch. Biochem. Biophys. 312:292-300(1994).
[10]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HEME AND OTHER
SUBUNITS OF THE BC1 COMPLEX, COFACTOR, TOPOLOGY, AND SUBUNIT.
PubMed=10873857; DOI=10.1016/S0969-2126(00)00152-0;
Hunte C., Koepke J., Lange C., Rossmanith T., Michel H.;
"Structure at 2.3 A resolution of the cytochrome bc1 complex from the
yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv
fragment.";
Structure 8:669-684(2000).
[11]
X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) IN COMPLEX WITH HEME AND OTHER
SUBUNITS OF THE BC1 COMPLEX, COFACTOR, TOPOLOGY, AND SUBUNIT.
PubMed=11880631; DOI=10.1073/pnas.052704699;
Lange C., Hunte C.;
"Crystal structure of the yeast cytochrome bc1 complex with its bound
substrate cytochrome c.";
Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002).
-!- FUNCTION: Component of the ubiquinol-cytochrome c reductase
complex (complex III or cytochrome b-c1 complex) that is part of
the mitochondrial respiratory chain. The b-c1 complex mediates
electron transfer from ubiquinol to cytochrome c. Contributes to
the generation of a proton gradient across the mitochondrial
membrane that is then used for ATP synthesis.
{ECO:0000269|PubMed:2551731, ECO:0000269|PubMed:8031140}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631};
Note=Binds 2 heme groups non-covalently.
{ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631};
-!- SUBUNIT: Fungal cytochrome b-c1 complex contains 10 subunits; 3
respiratory subunits, 2 core proteins and 5 low-molecular weight
proteins. Cytochrome b-c1 complex is a homodimer.
{ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
ECO:0000269|PubMed:8031140}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:8031140}; Multi-pass membrane protein
{ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
ECO:0000269|PubMed:8031140}.
-!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs
at about 562 nm, and heme 2 (or BH or b566) is high-potential and
absorbs at about 566 nm. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cytochrome b family.
{ECO:0000255|PROSITE-ProRule:PRU00967, ECO:0000255|PROSITE-
ProRule:PRU00968}.
-!- CAUTION: The protein contains only eight transmembrane helices,
not nine as predicted by bioinformatics tools.
{ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631}.
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EMBL; V00696; CAA24073.2; ALT_SEQ; Genomic_DNA.
EMBL; X84042; CAA58861.1; -; mRNA.
EMBL; KP263414; AIZ98890.1; -; Genomic_DNA.
EMBL; J01473; AAA32151.2; -; Genomic_DNA.
EMBL; J01472; AAA32151.2; JOINED; Genomic_DNA.
EMBL; J01475; AAA32152.2; -; Genomic_DNA.
EMBL; J01474; AAA32152.2; JOINED; Genomic_DNA.
PIR; A00159; CBBY.
PIR; S78660; S78660.
RefSeq; NP_009315.1; NC_001224.1.
PDB; 1EZV; X-ray; 2.30 A; C=1-385.
PDB; 1KB9; X-ray; 2.30 A; C=1-385.
PDB; 1KYO; X-ray; 2.97 A; C/N=1-385.
PDB; 1P84; X-ray; 2.50 A; C=1-385.
PDB; 2IBZ; X-ray; 2.30 A; C=1-385.
PDB; 3CX5; X-ray; 1.90 A; C/N=1-385.
PDB; 3CXH; X-ray; 2.50 A; C/N=1-385.
PDB; 4PD4; X-ray; 3.04 A; C=1-385.
PDBsum; 1EZV; -.
PDBsum; 1KB9; -.
PDBsum; 1KYO; -.
PDBsum; 1P84; -.
PDBsum; 2IBZ; -.
PDBsum; 3CX5; -.
PDBsum; 3CXH; -.
PDBsum; 4PD4; -.
ProteinModelPortal; P00163; -.
SMR; P00163; -.
BioGrid; 34779; 33.
ComplexPortal; CPX-567; Mitochondrial electron transport complex III.
IntAct; P00163; 3.
STRING; 4932.Q0105; -.
TCDB; 3.D.3.3.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
PaxDb; P00163; -.
PRIDE; P00163; -.
TopDownProteomics; P00163; -.
EnsemblFungi; Q0105; Q0105; Q0105.
GeneID; 854583; -.
KEGG; sce:Q0105; -.
EuPathDB; FungiDB:Q0105; -.
SGD; S000007270; COB.
GeneTree; ENSGT00390000017948; -.
HOGENOM; HOG000255206; -.
InParanoid; P00163; -.
KO; K00412; -.
OMA; HETGSNN; -.
OrthoDB; EOG092C2QFL; -.
BioCyc; YEAST:Q0105-MONOMER; -.
EvolutionaryTrace; P00163; -.
PRO; PR:P00163; -.
Proteomes; UP000002311; Mitochondrion.
GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:UniProtKB.
GO; GO:0045153; F:electron transporter, transferring electrons within CoQH2-cytochrome c reductase complex activity; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IDA:UniProtKB.
GO; GO:0009060; P:aerobic respiration; IMP:SGD.
GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IDA:UniProtKB.
CDD; cd00290; cytochrome_b_C; 1.
CDD; cd00284; Cytochrome_b_N; 1.
Gene3D; 1.20.810.10; -; 1.
InterPro; IPR005798; Cyt_b/b6_C.
InterPro; IPR036150; Cyt_b/b6_C_sf.
InterPro; IPR005797; Cyt_b/b6_N.
InterPro; IPR027387; Cytb/b6-like_sf.
InterPro; IPR030689; Cytochrome_b.
InterPro; IPR016174; Di-haem_cyt_TM.
Pfam; PF00032; Cytochrom_B_C; 1.
Pfam; PF00033; Cytochrome_B; 1.
PIRSF; PIRSF038885; COB; 1.
SUPFAM; SSF81342; SSF81342; 1.
SUPFAM; SSF81648; SSF81648; 1.
PROSITE; PS51003; CYTB_CTER; 1.
PROSITE; PS51002; CYTB_NTER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Electron transport; Heme; Iron; Membrane; Metal-binding;
Mitochondrion; Mitochondrion inner membrane; Reference proteome;
Respiratory chain; Transmembrane; Transmembrane helix; Transport;
Ubiquinone.
CHAIN 1 385 Cytochrome b.
/FTId=PRO_0000061769.
TRANSMEM 32 52 Helical. {ECO:0000244|PDB:1EZV,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
TRANSMEM 76 98 Helical. {ECO:0000244|PDB:1EZV,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
TRANSMEM 113 133 Helical. {ECO:0000244|PDB:1EZV,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
TRANSMEM 179 199 Helical. {ECO:0000244|PDB:1EZV,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
TRANSMEM 225 245 Helical. {ECO:0000244|PDB:1EZV,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
TRANSMEM 289 309 Helical. {ECO:0000244|PDB:1EZV,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
TRANSMEM 321 341 Helical. {ECO:0000244|PDB:1EZV,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
TRANSMEM 348 368 Helical. {ECO:0000244|PDB:1EZV,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
METAL 82 82 Iron 1 (heme b562 axial ligand).
{ECO:0000244|PDB:1EZV,
ECO:0000244|PDB:1KB9,
ECO:0000244|PDB:1KYO,
ECO:0000244|PDB:1P84,
ECO:0000244|PDB:2IBZ,
ECO:0000244|PDB:3CX5,
ECO:0000244|PDB:3CXH,
ECO:0000244|PDB:4PD4,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
METAL 96 96 Iron 2 (heme b566 axial ligand).
{ECO:0000244|PDB:1EZV,
ECO:0000244|PDB:1KB9,
ECO:0000244|PDB:1KYO,
ECO:0000244|PDB:1P84,
ECO:0000244|PDB:2IBZ,
ECO:0000244|PDB:3CX5,
ECO:0000244|PDB:3CXH,
ECO:0000244|PDB:4PD4,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
METAL 183 183 Iron 1 (heme b562 axial ligand).
{ECO:0000244|PDB:1EZV,
ECO:0000244|PDB:1KB9,
ECO:0000244|PDB:1KYO,
ECO:0000244|PDB:1P84,
ECO:0000244|PDB:2IBZ,
ECO:0000244|PDB:3CX5,
ECO:0000244|PDB:3CXH,
ECO:0000244|PDB:4PD4,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
METAL 197 197 Iron 2 (heme b566 axial ligand).
{ECO:0000244|PDB:1EZV,
ECO:0000244|PDB:1KB9,
ECO:0000244|PDB:1KYO,
ECO:0000244|PDB:1P84,
ECO:0000244|PDB:2IBZ,
ECO:0000244|PDB:3CX5,
ECO:0000244|PDB:3CXH,
ECO:0000244|PDB:4PD4,
ECO:0000269|PubMed:10873857,
ECO:0000269|PubMed:11880631}.
BINDING 202 202 Ubiquinone.
{ECO:0000250|UniProtKB:P00157}.
VARIANT 131 131 G -> S (in mutant W7 which is respiratory
deficient).
CONFLICT 122 122 I -> T (in Ref. 3; CAA58861 and 6;
AAA32151). {ECO:0000305}.
CONFLICT 269 269 I -> ID (in Ref. 1; CAA24073 and 2; no
nucleotide entry). {ECO:0000305}.
HELIX 3 6 {ECO:0000244|PDB:3CX5}.
HELIX 10 17 {ECO:0000244|PDB:3CX5}.
STRAND 21 23 {ECO:0000244|PDB:3CX5}.
HELIX 28 31 {ECO:0000244|PDB:3CX5}.
HELIX 32 51 {ECO:0000244|PDB:3CX5}.
TURN 58 60 {ECO:0000244|PDB:3CX5}.
HELIX 61 70 {ECO:0000244|PDB:3CX5}.
HELIX 75 102 {ECO:0000244|PDB:3CX5}.
TURN 103 106 {ECO:0000244|PDB:3CX5}.
TURN 108 110 {ECO:0000244|PDB:1KYO}.
HELIX 111 135 {ECO:0000244|PDB:3CX5}.
HELIX 138 149 {ECO:0000244|PDB:3CX5}.
HELIX 150 153 {ECO:0000244|PDB:3CX5}.
TURN 155 157 {ECO:0000244|PDB:3CX5}.
HELIX 158 166 {ECO:0000244|PDB:3CX5}.
STRAND 168 171 {ECO:0000244|PDB:3CX5}.
HELIX 173 204 {ECO:0000244|PDB:3CX5}.
STRAND 217 220 {ECO:0000244|PDB:3CX5}.
TURN 221 223 {ECO:0000244|PDB:3CX5}.
HELIX 224 246 {ECO:0000244|PDB:3CX5}.
TURN 248 251 {ECO:0000244|PDB:3CX5}.
HELIX 254 257 {ECO:0000244|PDB:3CX5}.
HELIX 273 275 {ECO:0000244|PDB:3CX5}.
HELIX 276 283 {ECO:0000244|PDB:3CX5}.
STRAND 285 287 {ECO:0000244|PDB:3CX5}.
HELIX 288 300 {ECO:0000244|PDB:3CX5}.
HELIX 301 304 {ECO:0000244|PDB:3CX5}.
HELIX 305 308 {ECO:0000244|PDB:3CX5}.
STRAND 312 316 {ECO:0000244|PDB:3CX5}.
HELIX 320 340 {ECO:0000244|PDB:3CX5}.
HELIX 348 364 {ECO:0000244|PDB:3CX5}.
HELIX 366 380 {ECO:0000244|PDB:3CX5}.
SEQUENCE 385 AA; 43656 MW; 1B1B1616BBC2A798 CRC64;
MAFRKSNVYL SLVNSYIIDS PQPSSINYWW NMGSLLGLCL VIQIVTGIFM AMHYSSNIEL
AFSSVEHIMR DVHNGYILRY LHANGASFFF MVMFMHMAKG LYYGSYRSPR VTLWNVGVII
FILTIATAFL GYCCVYGQMS HWGATVITNL FSAIPFVGND IVSWLWGGFS VSNPTIQRFF
ALHYLVPFII AAMVIMHLMA LHIHGSSNPL GITGNLDRIP MHSYFIFKDL VTVFLFMLIL
ALFVFYSPNT LGHPDNYIPG NPLVTPASIV PEWYLLPFYA ILRSIPDKLL GVITMFAAIL
VLLVLPFTDR SVVRGNTFKV LSKFFFFIFV FNFVLLGQIG ACHVEVPYVL MGQIATFIYF
AYFLIIVPVI STIENVLFYI GRVNK


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