CYB_PARDE
ID CYB_PARDE Reviewed; 440 AA.
AC P05418;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cytochrome b;
GN Name=petB;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2820981; DOI=10.1016/s0021-9258(19)76497-7;
RA Kurowski B., Ludwig B.;
RT "The genes of the Paracoccus denitrificans bc1 complex. Nucleotide sequence
RT and homologies between bacterial and mitochondrial subunits.";
RL J. Biol. Chem. 262:13805-13811(1987).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex), which is a respiratory chain
CC that generates an electrochemical potential coupled to ATP synthesis.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 2 heme b groups non-covalently. {ECO:0000250};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; M17522; AAA25572.1; -; Genomic_DNA.
DR EMBL; X05799; CAA29244.1; -; Genomic_DNA.
DR PIR; B29413; B29413.
DR RefSeq; WP_011748590.1; NZ_PPGA01000003.1.
DR PDB; 2YIU; X-ray; 2.70 A; A/D=1-440.
DR PDBsum; 2YIU; -.
DR AlphaFoldDB; P05418; -.
DR SMR; P05418; -.
DR TCDB; 3.D.3.1.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR OMA; RFFAFHF; -.
DR BRENDA; 7.1.1.8; 3341.
DR GO; GO:0005886; C:plasma 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..440
FT /note="Cytochrome b"
FT /id="PRO_0000061771"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 97
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 BINDING 111
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 BINDING 198
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 BINDING 212
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 HELIX 14..22
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 47..66
FT /evidence="ECO:0007829|PDB:2YIU"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 90..118
FT /evidence="ECO:0007829|PDB:2YIU"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 126..148
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:2YIU"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 188..219
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 244..269
FT /evidence="ECO:0007829|PDB:2YIU"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:2YIU"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 328..344
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 363..381
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 389..405
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 424..429
FT /evidence="ECO:0007829|PDB:2YIU"
SQ SEQUENCE 440 AA; 50116 MW; 8D211B8614920C63 CRC64;
MAGIPHDHYE PKTGFERWLH RRLPIVSLVY DTLMIPTPKN LNWWWIWGIV LAFCLVLQIA
TGIVLVMHYT PHVDLAFASV EHIMRDVNGG YMLRYLHANG ASLFFLAVYI HIFRGLYYGS
YKAPREVTWI VGMLIYLMMM GTAFMGYVLP WGQMSFWGAT VITGLFGAIP GVGEAIQTWL
LGGPAVDNPT LNRFFSLHYL LPFVIAALVV VHIWAFHTTG NNNPTGVEVR RGSKEEAKKD
TLPFWPYFVI KDLFALAVVL VVFFAIVGFM PNYLGHPDNY IEANPLVTPA HIVPEWYFLP
FYAILRAFTA DVWVVMLVNW LSFGIIDAKF FGVIAMFGAI LVMALVPWLD TSRVRSGQYR
PLFKWWFWLL AVDFVVLMWV GAMPAEGIYP YIALAGSAYW FAYFLIILPL LGIIEKPDAM
PQTIEEDFNA HYGPETHPAE
