ID Q6R9D5_MAIZE Unreviewed; 388 AA.
AC Q6R9D5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117};
GN Name=cob {ECO:0000313|EMBL:AAR91052.1};
GN Synonyms=4055802 {ECO:0000313|EnsemblPlants:Zm00001eb126090_P001};
OS Zea mays (Maize).
OG Mitochondrion {ECO:0000313|EMBL:AAR91052.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AAR91052.1, ECO:0000313|Proteomes:UP000007305};
RN [1] {ECO:0000313|EMBL:AAR91052.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NB {ECO:0000313|EMBL:AAR91052.1};
RA Clifton S., Fauron C., Gibson M., Minx P., Newton K., Rugen M., Spieth J.,
RA Sun H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAR91052.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. B37N {ECO:0000313|Proteomes:UP000007305}, and NB
RC {ECO:0000313|EMBL:AAR91052.1};
RX PubMed=15542500; DOI=10.1104/pp.104.044602;
RA Clifton S.W., Minx P., Fauron C.M.-R., Gibson M., Allen J.O., Sun H.,
RA Thompson M., Barbazuk W.B., Kanuganti S., Tayloe C., Meyer L., Wilson R.K.,
RA Newton K.J.;
RT "Sequence and comparative analysis of the maize NB mitochondrial genome.";
RL Plant Physiol. 136:3486-3503(2004).
RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb187520_P001, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb187520_P001,
RC ECO:0000313|Proteomes:UP000007305};
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [4] {ECO:0000313|EnsemblPlants:Zm00001eb126090_P001, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb126090_P001,
RC ECO:0000313|Proteomes:UP000007305};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EnsemblPlants:Zm00001eb126090_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb126090_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
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:0000256|RuleBase:RU362117}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|RuleBase:RU362117};
CC Note=Binds 2 heme groups non-covalently.
CC {ECO:0000256|RuleBase:RU362117};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004448}.
CC -!- SIMILARITY: Belongs to the cytochrome b family.
CC {ECO:0000256|RuleBase:RU362117}.
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DR EMBL; AY506529; AAR91052.1; -; Genomic_DNA.
DR RefSeq; YP_588373.1; NC_007982.1.
DR AlphaFoldDB; Q6R9D5; -.
DR SMR; Q6R9D5; -.
DR STRING; 4577.Q6R9D5; -.
DR EnsemblPlants; Zm00001eb126090_T001; Zm00001eb126090_P001; Zm00001eb126090.
DR EnsemblPlants; Zm00001eb187520_T001; Zm00001eb187520_P001; Zm00001eb187520.
DR EnsemblPlants; Zm00001eb436400_T001; Zm00001eb436400_P001; Zm00001eb436400.
DR EnsemblPlants; Zm00001eb438850_T001; Zm00001eb438850_P001; Zm00001eb438850.
DR EnsemblPlants; Zm00001eb440640_T001; Zm00001eb440640_P001; Zm00001eb440640.
DR GeneID; 4055802; -.
DR Gramene; Zm00001eb126090_T001; Zm00001eb126090_P001; Zm00001eb126090.
DR Gramene; Zm00001eb187520_T001; Zm00001eb187520_P001; Zm00001eb187520.
DR Gramene; Zm00001eb436400_T001; Zm00001eb436400_P001; Zm00001eb436400.
DR Gramene; Zm00001eb438850_T001; Zm00001eb438850_P001; Zm00001eb438850.
DR Gramene; Zm00001eb440640_T001; Zm00001eb440640_P001; Zm00001eb440640.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; Q6R9D5; -.
DR OMA; NISAWWN; -.
DR OrthoDB; 232320at2759; -.
DR Proteomes; UP000007305; Chromosome 3.
DR Proteomes; UP000007305; Chromosome 4.
DR Proteomes; UP000007305; Mitochondrion.
DR ExpressionAtlas; Q6R9D5; baseline.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR CDD; cd00290; cytochrome_b_C; 1.
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; IPR048260; Cytochrome_b_C_euk/bac.
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; 1.
DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
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:RU362117};
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|RuleBase:RU362117};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038885-2};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU362117};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|RuleBase:RU362117};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362117};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362117};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362117}.
FT TRANSMEM 34..61
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 82..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 146..171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 191..210
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 231..252
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 352..374
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT DOMAIN 1..216
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT DOMAIN 217..386
FT /note="Cytochrome b/b6 C-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51003"
FT BINDING 88
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 102
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 189
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 203
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 208
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1"
SQ SEQUENCE 388 AA; 43551 MW; 34A4F62ED52C4DB3 CRC64;
MTIRNQRFSL LKQPIYSTLN QHLIDYPTPS NLSYWWGFGS LAGICLVIQI VTGVFLAMHY
TPHVDLAFNS VEHIMRDVEG GWLLRYMHAN GASMFLIVVH LHIFRGLYHA SYSSPREFVW
CLGVVIFLLM IVTAFIGYVP PWGQMSFWGA TVITSLASAI PVVGDTIVTW LWGGFSVDNA
TLNRFFSLHH LLPLILAGAS LLHLAALHQY GSNNPLGVHS EMDKIASYPY FYVKDLVGRV
ASAIFFSIWI FFAPNVLGHP DNYIPANPMP TPPHIVPEWY FLPIHAILRS IPDKAGGVAA
IAPVFISLLA LPFFKEMYVR SSSFRPIHQG IFWLLLADCL LLGWIGCQPV EAPFVTIGQI
SSFFFFLFFA ITPIPGRVGR GIPKYYTE
//
