CYB_NEUCR
ID CYB_NEUCR Reviewed; 385 AA.
AC Q35128; M1R9S0; P00162; Q35132; Q95857;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cytochrome b;
DE EC=7.1.1.8 {ECO:0000269|PubMed:1847681, ECO:0000269|PubMed:3015618};
DE AltName: Full=Complex III subunit 3;
DE AltName: Full=Complex III subunit III {ECO:0000303|PubMed:6302289};
DE AltName: Full=Cytochrome b-c1 complex subunit 3;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase complex cytochrome b subunit;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 30 kDa protein;
GN Name=cob; Synonyms=cytb; ORFNames=NCM030, NCU16013;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=10872314; DOI=10.1002/j.1460-2075.1983.tb01575.x;
RA Helmer-Citterich M., Morelli G., Macino G.;
RT "Nucleotide sequence and intron structure of the apocytochrome b gene of
RT Neurospora crassa mitochondria.";
RL EMBO J. 2:1235-1242(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RA Kennell J.C., Collins R.A., Griffiths A.J.F., Nargang F.E.;
RT "Mitochondrial genetics of Neurospora.";
RL (In) Kueck U. (eds.);
RL The Mycota II, Genetics and Biotechnology (2nd edition), pp.95-112,
RL Springer-Verlag, Berlin-Heidelberg (2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-163.
RC STRAIN=Adiopodoume-1 / FGSC 430, and
RC ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=2963999; DOI=10.1093/nar/16.3.1125;
RA Collins R.A., Reynolds C.A., Olive J.;
RT "The self-splicing intron in the Neurospora apocytochrome b gene contains a
RT long reading frame in frame with the upstream exon.";
RL Nucleic Acids Res. 16:1125-1134(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-385.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=6231283; DOI=10.1016/s0021-9258(17)43690-8;
RA Burke J.M., Breitenberger C., Heckman J.E., Dujon B., RajBhandary U.L.;
RT "Cytochrome b gene of Neurospora crassa mitochondria. Partial sequence and
RT location of introns at sites different from those in Saccharomyces
RT cerevisiae and Aspergillus nidulans.";
RL J. Biol. Chem. 259:504-511(1984).
RN [6]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=226365; DOI=10.1111/j.1432-1033.1979.tb13240.x;
RA Weiss H., Kolb H.J.;
RT "Isolation of mitochondrial succinate: ubiquinone reductase, cytochrome c
RT reductase and cytochrome c oxidase from Neurospora crassa using nonionic
RT detergent.";
RL Eur. J. Biochem. 99:139-149(1979).
RN [7]
RP SUBUNIT.
RX PubMed=6273583; DOI=10.1016/0022-2836(81)90301-6;
RA Leonard K., Wingfield P., Arad T., Weiss H.;
RT "Three-dimensional structure of ubiquinol:cytochrome c reductase from
RT Neurospora mitochondria determined by electron microscopy of membrane
RT crystals.";
RL J. Mol. Biol. 149:259-274(1981).
RN [8]
RP SUBUNIT.
RX PubMed=18251112; DOI=10.1007/bf00744526;
RA Mendel-Hartvig I., Nelson B.D.;
RT "Comparative study of the peptide composition of Complex III (quinol-
RT cytochrome c reductase).";
RL J. Bioenerg. Biomembr. 15:289-299(1983).
RN [9]
RP SUBUNIT.
RX PubMed=6302289; DOI=10.1016/s0022-2836(83)80258-7;
RA Karlsson B., Hovmoeller S., Weiss H., Leonard K.;
RT "Structural studies of cytochrome reductase. Subunit topography determined
RT by electron microscopy of membrane crystals of a subcomplex.";
RL J. Mol. Biol. 165:287-302(1983).
RN [10]
RP FUNCTION OF COMPLEX III.
RX PubMed=3015618; DOI=10.1111/j.1432-1033.1986.tb09799.x;
RA Linke P., Bechmann G., Gothe A., Weiss H.;
RT "Dimeric ubiquinol:cytochrome c reductase of Neurospora mitochondria
RT contains one cooperative ubiquinone-reduction centre.";
RL Eur. J. Biochem. 158:615-621(1986).
RN [11]
RP FUNCTION OF COMPLEX III.
RX PubMed=1847681; DOI=10.1111/j.1432-1033.1991.tb15722.x;
RA Bechmann G., Weiss H.;
RT "Regulation of the proton/electron stoichiometry of mitochondrial
RT ubiquinol:cytochrome c reductase by the membrane potential.";
RL Eur. J. Biochem. 195:431-438(1991).
RN [12]
RP SUBUNIT.
RX PubMed=17873079; DOI=10.1128/ec.00149-07;
RA Marques I., Dencher N.A., Videira A., Krause F.;
RT "Supramolecular organization of the respiratory chain in Neurospora crassa
RT mitochondria.";
RL Eukaryot. Cell 6:2391-2405(2007).
RN [13]
RP FUNCTION OF COMPLEX III, AND SUBUNIT.
RX PubMed=19239619; DOI=10.1111/j.1365-2958.2009.06643.x;
RA Duarte M., Videira A.;
RT "Effects of mitochondrial complex III disruption in the respiratory chain
RT of Neurospora crassa.";
RL Mol. Microbiol. 72:246-258(2009).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c (PubMed:3015618) (Probable). Cytochrome b is a
CC catalytic core subunit containing 2 b-type hemes BL and BH
CC topographically segregated in the quinone reduction (Qi) and quinol
CC oxidation (Q0) sites on opposite sides of the membrane (By similarity).
CC {ECO:0000250|UniProtKB:P00163, ECO:0000269|PubMed:3015618,
CC ECO:0000305|PubMed:1847681, ECO:0000305|PubMed:19239619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000269|PubMed:1847681,
CC ECO:0000269|PubMed:3015618};
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 per subunit.
CC {ECO:0000250|UniProtKB:P00163};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 10 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b (cob), cytochrome c1 (cyt-1) and Rieske protein
CC (fes-1), 2 core protein subunits pep and ucr-1, and 5 low-molecular
CC weight protein subunits qcr6, qcr7, qcr8, qcr9 and probably
CC NCU16844/qcr10 (PubMed:226365, PubMed:6273583, PubMed:18251112,
CC PubMed:6302289). The complex exists as an obligatory dimer and forms
CC supercomplexes (SCs) in the inner mitochondrial membrane with NADH-
CC ubiquinone oxidoreductase (complex I, CI) and cytochrome c oxidase
CC (complex IV, CIV), resulting in different assemblies (supercomplexes
CC SCI(1)III(2), SCIII(2)IV(1) and SCIII(2)IV(2) as well as higher order
CC I(x)III(y)IV(z) megacomplexes) (PubMed:17873079, PubMed:19239619).
CC {ECO:0000269|PubMed:17873079, ECO:0000269|PubMed:18251112,
CC ECO:0000269|PubMed:19239619, ECO:0000269|PubMed:226365,
CC ECO:0000269|PubMed:6273583, ECO:0000269|PubMed:6302289}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:226365}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00163}.
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}.
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DR EMBL; M37324; AAA31961.2; -; Genomic_DNA.
DR EMBL; KC683708; AGG16002.1; -; Genomic_DNA.
DR EMBL; X06884; CAB37296.1; -; Genomic_DNA.
DR EMBL; K01181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A00158; CBNC.
DR RefSeq; YP_009126714.1; NC_026614.1.
DR AlphaFoldDB; Q35128; -.
DR SMR; Q35128; -.
DR STRING; 367110.Q35128; -.
DR EnsemblFungi; AGG16002; AGG16002; NCU16013.
DR GeneID; 23681566; -.
DR KEGG; ncr:NCU16013; -.
DR VEuPathDB; FungiDB:NCU16013; -.
DR InParanoid; Q35128; -.
DR Proteomes; UP000001805; Mitochondrion.
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:UniProtKB-EC.
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 1: Evidence at protein level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..385
FT /note="Cytochrome b"
FT /id="PRO_0000061749"
FT TOPO_DOM 1..27
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 28..51
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TOPO_DOM 52..74
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 75..102
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TOPO_DOM 103..110
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 111..135
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TOPO_DOM 136..172
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 173..205
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TOPO_DOM 206..224
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 225..247
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TOPO_DOM 248..288
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TOPO_DOM 310..320
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TOPO_DOM 342..348
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 349..365
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TOPO_DOM 366..385
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT BINDING 16
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT BINDING 82
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 96
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 183
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 197
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 202
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT CONFLICT 164..166
FT /note="FIW -> LHL (in Ref. 1; AAA31961)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="H -> Y (in Ref. 1; AAA31961)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="P -> L (in Ref. 1; AAA31961)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..192
FT /note="AA -> VV (in Ref. 1; AAA31961)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="H -> Y (in Ref. 1; AAA31961)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..207
FT /note="ALHDTAGS -> VLYDIVGL (in Ref. 1; AAA31961)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..214
FT /note="VS -> AL (in Ref. 1; AAA31961)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="T -> I (in Ref. 1; AAA31961)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="Y -> D (in Ref. 1; AAA31961)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="F -> L (in Ref. 1; AAA31961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43524 MW; 15F45E399F214CDF CRC64;
MRLLKSHPLL KLVNSYLIDA SQPSNISYLW NFGSLLACCL IIQIVTGVTL AMHYSPNVLE
AFNSIEHIMR DVNNGWLVRY LHSNTASAFF FLVYLHIGRG MYYGSYRAPR TLVWAIGTVI
LILMMATAFL GYVLPYGQMS LWGATVITNL ISAIPWIGQD IVEFIWGGFS VNNATLNRFF
ALHFVLPFIL AALVLMHLIA LHDTAGSSNP LGVSGNYDRI TFAPYYLFKD LITIFIFIYV
LSSFVFFMPN VLGDSENYIM ANPMQTPPAI VPEWYLLPFY AILRSIPNKL LGVIAMFSAI
LAIMLLPITD LGRSKGLQFR PLSKFAFWAF VVNFLILMKL GACHVESPFI ELGQFSTIFY
FSYFIFIVPV LSLIENTLVD LNYLK
