ID A0A1I7FUD3_9BURK Unreviewed; 473 AA.
AC A0A1I7FUD3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU003385};
GN ORFNames=SAMN04489707_100352 {ECO:0000313|EMBL:SFU39760.1};
OS Paenacidovorax caeni.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paenacidovorax.
OX NCBI_TaxID=343013 {ECO:0000313|EMBL:SFU39760.1, ECO:0000313|Proteomes:UP000183656};
RN [1] {ECO:0000313|EMBL:SFU39760.1, ECO:0000313|Proteomes:UP000183656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-24608 {ECO:0000313|EMBL:SFU39760.1,
RC ECO:0000313|Proteomes:UP000183656};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002444, ECO:0000256|RuleBase:RU003385}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|RuleBase:RU003385};
CC Note=Binds 2 heme groups non-covalently.
CC {ECO:0000256|RuleBase:RU003385};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR038885-2};
CC Note=Binds 2 heme groups non-covalently.
CC {ECO:0000256|PIRSR:PIRSR038885-2};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000256|ARBA:ARBA00011649,
CC ECO:0000256|RuleBase:RU003385}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome b family.
CC {ECO:0000256|RuleBase:RU003385}.
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DR EMBL; FPBX01000003; SFU39760.1; -; Genomic_DNA.
DR RefSeq; WP_054254705.1; NZ_FPBX01000003.1.
DR AlphaFoldDB; A0A1I7FUD3; -.
DR STRING; 343013.SAMN04489707_100352; -.
DR OrthoDB; 9804503at2; -.
DR Proteomes; UP000183656; Unassembled WGS sequence.
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; cd00284; Cytochrome_b_N; 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; IPR048259; Cytochrome_b_N_euk/bac.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR PANTHER; PTHR19271; CYTOCHROME B; 1.
DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 1.
DR PIRSF; PIRSF038885; COB; 2.
DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 2.
DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU003385};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038885-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038885-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038885-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000183656};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|RuleBase:RU003385};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003385};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003385}.
FT TRANSMEM 50..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..233
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT DOMAIN 246..466
FT /note="Cytochrome b/b6 C-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51003"
FT BINDING 104
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:0000256|PIRSR:PIRSR038885-2"
FT BINDING 118
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:0000256|PIRSR:PIRSR038885-2"
FT BINDING 205
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:0000256|PIRSR:PIRSR038885-2"
FT BINDING 220
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:0000256|PIRSR:PIRSR038885-2"
FT BINDING 225
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1"
SQ SEQUENCE 473 AA; 53075 MW; 3982BCADC65E3BCD CRC64;
MAAYREFKEL SPNASAGAKL TNWFENRFPT AFDAYKVHMS EYYAPKNFNF WYIFGSLALL
VLVIQIVTGI FLVMHYKPDA AKAFESVEYI MRDVPWGWLI RYMHSTGASA FFVVVYLHMF
RGLLYGSYRK PRELVWIFGC AIFLALMAEA FMGYLLPWGQ MSYWGAQVIV NLFSAIPFVG
PDLALLIRGD YVVGDATLNR FFSFHVIAVP LVLIGLVVAH LLALHDVGSN NPDGIEIKGP
GKPVDAKGHP LDGIPFHPYY TVHDIFGVGV FLFIFSAVVF FAPELGGYFL EYNNFIPADP
LKTPNHIAPV WYFTPFYSML RAITSEMMYA LIACVVLGAG FGVLKAKLPG FIKGGIVVAA
AVVIALMLSI DAKFWGVVVM GGAVIILFFL PWLDQSPARS IRYRPGWHTW LYAVFVVVFV
ILAYLGVQPP SPVGERVSQV GTLFYFGFFL LMPWWTRLGT PKPVPDRVTF KPH
//
