CYB_ELANI
ID CYB_ELANI Reviewed; 371 AA.
AC Q9MLK8;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Elapsoidea nigra (Usambara garter snake).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Elapsoidea.
OX NCBI_TaxID=66178;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10764543; DOI=10.1006/mpev.1999.0725;
RA Slowinski J.B., Keogh J.S.;
RT "Phylogenetic relationships of elapid snakes based on cytochrome b mtDNA
RT sequences.";
RL Mol. Phylogenet. Evol. 15:157-164(2000).
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:P00157}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P00157};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:P00157};
CC -!- SUBUNIT: The cytochrome bc1 complex contains 3 respiratory subunits
CC (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and
CC probably 6 low-molecular weight proteins.
CC {ECO:0000250|UniProtKB:P00157}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00157}.
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 full-length protein contains only eight transmembrane
CC helices, not nine as predicted by bioinformatics tools.
CC {ECO:0000250|UniProtKB:P00157}.
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DR EMBL; AF217820; AAF37239.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9MLK8; -.
DR SMR; Q9MLK8; -.
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 3: Inferred from homology;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..371
FT /note="Cytochrome b"
FT /id="PRO_0000060907"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 69..90
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 339..358
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 75
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:P00157"
FT BINDING 89
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:P00157"
FT BINDING 174
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:P00157"
FT BINDING 188
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:P00157"
FT BINDING 193
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
SQ SEQUENCE 371 AA; 42188 MW; F6AC3105F4F6EA22 CRC64;
MSNQHTLLMT NLLPVGSNIS TWWNFGSMLL TCLALQTMTG FFLAIHYTAN INLAFASVIH
ITRDIPYGWT MQSLHAIGAS LFFICIYIHI ARGLYYGLYM NKEVWLSGIT LLFTLMATAF
FGYVLPWGQM SFWAATVITN LLTAIPYLGT MLTTWLWGGF SINDPTLTRF FALHFILPFI
IISLSSAHIM LLHTEGSNNP LGTNSDIDKI PFHPYHSNKD MLTATIMITM LFITLSFLPN
LLNDPENFSK ANPMITPQHI KPEWYFLFAY GILRSIPNKL GGTLALLTSV MILATTPFTH
TSHIRSMTFR PMTQTLFWIL IATLITITWT ATKPVEPPFM FISQMASMIY FSFFFMNPLL
GWTENKIMMN N
