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Database: UniProt
Entry: B4F892_MAIZE
LinkDB: B4F892_MAIZE
Original site: B4F892_MAIZE 
ID   B4F892_MAIZE            Unreviewed;       272 AA.
AC   B4F892;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial {ECO:0000256|RuleBase:RU004494};
DE            EC=7.1.1.8 {ECO:0000256|RuleBase:RU004494};
GN   ORFNames=ZEAMMB73_Zm00001d016619 {ECO:0000313|EMBL:AQK71309.1};
OS   Zea mays (Maize).
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:ACF78335.1};
RN   [1] {ECO:0000313|EMBL:ACG35467.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
RN   [2] {ECO:0000313|EMBL:ACF78335.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACF78335.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [3] {ECO:0000313|EMBL:AQK71309.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK71309.1};
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.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00029351,
CC         ECO:0000256|RuleBase:RU004494};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|RuleBase:RU004494};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU004494};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004434}.
CC   -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC       {ECO:0000256|RuleBase:RU004494}.
CC   -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC       {ECO:0000256|ARBA:ARBA00010651}.
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DR   EMBL; BT033330; ACF78335.1; -; mRNA.
DR   EMBL; BT034451; ACF79456.1; -; mRNA.
DR   EMBL; BT043038; ACF88043.1; -; mRNA.
DR   EMBL; EU963349; ACG35467.1; -; mRNA.
DR   EMBL; EU964044; ACG36162.1; -; mRNA.
DR   EMBL; CM000781; AQK71309.1; -; Genomic_DNA.
DR   RefSeq; NP_001131160.1; NM_001137688.1.
DR   AlphaFoldDB; B4F892; -.
DR   SMR; B4F892; -.
DR   IntAct; B4F892; 9.
DR   STRING; 4577.B4F892; -.
DR   PaxDb; 4577-AC214350-3_FGP007; -.
DR   GeneID; 100192468; -.
DR   KEGG; zma:100192468; -.
DR   eggNOG; KOG1671; Eukaryota.
DR   HOGENOM; CLU_055690_0_0_1; -.
DR   InParanoid; B4F892; -.
DR   OrthoDB; 166674at2759; -.
DR   ExpressionAtlas; B4F892; baseline and differential.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   CDD; cd03470; Rieske_cytochrome_bc1; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   InterPro; IPR004192; Rieske_TM.
DR   InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR   NCBIfam; TIGR01416; Rieske_proteo; 1.
DR   PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10134:SF20; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF02921; UCR_TM; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   SUPFAM; SSF81502; ISP transmembrane anchor; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|RuleBase:RU004494};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|RuleBase:RU004495};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW   ECO:0000256|RuleBase:RU004495};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|RuleBase:RU004494}.
FT   DOMAIN          202..270
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   272 AA;  29684 MW;  D7A179015B356F66 CRC64;
     MLRVAGRRLS SALAWRPAAA ASGSRGPLAG TLPGRDDDDT RDCRARFAIE SPFFAAARGF
     SAETLAPRNQ DVGLSELPAT VAAVKNPSGK IVYDEYNHER YPPGDPSKRA FAYFVLSGGR
     FIYASLLRLL VLKFVLSMSA SKDVLALASL EVDLSSIEPG TTVTVKWRGK PVFIRRRTED
     DIKLANSVDV ASLRHPEQDA ERVKNPEWLV VIGVCTHLGC IPLPNAGDFG GWFCPCHGSH
     YDISGRIRKG PAPFNLEVPT YSFLEENKLL IG
//
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