UCRI5_TOBAC
ID UCRI5_TOBAC Reviewed; 268 AA.
AC P51135;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cytochrome b-c1 complex subunit Rieske-5, mitochondrial;
DE EC=7.1.1.8;
DE AltName: Full=Complex III subunit 5-5;
DE AltName: Full=Rieske iron-sulfur protein 5;
DE Short=RISP5;
DE AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit 5;
DE Flags: Precursor;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. SC58; TISSUE=Flower;
RX PubMed=8180500; DOI=10.2307/3869763;
RA Huang J., Struck F., Matzinger D.F., Levings C.S. III;
RT "Flower-enhanced expression of a nuclear-encoded mitochondrial respiratory
RT protein is associated with changes in mitochondrion number.";
RL Plant Cell 6:439-448(1994).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c. The Rieske protein is a catalytic core subunit
CC containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2
CC conformational states during catalysis to transfer electrons from the
CC quinol bound in the Q(0) site in cytochrome b to cytochrome c1.
CC {ECO:0000250|UniProtKB:P08067}.
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:0000250|UniProtKB:P08067};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 3 respiratory subunits cytochrome b, cytochrome c1 and
CC Rieske protein, 2 core protein subunits, and several low-molecular
CC weight protein subunits. The complex exists as an obligatory dimer and
CC forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC cytochrome c oxidase (complex IV, CIV). {ECO:0000250|UniProtKB:P08067}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P08067}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P08067}.
CC -!- TISSUE SPECIFICITY: High levels are seen in the flowers while a low
CC level expression is seen in the roots, leaves and stems.
CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000305}.
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DR EMBL; L16813; AAA20834.1; -; mRNA.
DR PIR; T02023; T02023.
DR RefSeq; NP_001312589.1; NM_001325660.1.
DR AlphaFoldDB; P51135; -.
DR SMR; P51135; -.
DR STRING; 4097.P51135; -.
DR GeneID; 107798995; -.
DR KEGG; nta:107798995; -.
DR OMA; FSSVSWR; -.
DR PhylomeDB; P51135; -.
DR Proteomes; UP000084051; Unplaced.
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 Gene3D; 2.102.10.10; -; 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 PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF02921; UCR_TM; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR TIGRFAMs; TIGR01416; Rieske_proteo; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 57..268
FT /note="Cytochrome b-c1 complex subunit Rieske-5,
FT mitochondrial"
FT /id="PRO_0000030680"
FT TOPO_DOM 57..105
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..268
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT DOMAIN 178..266
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 211
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 213
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 230
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 233
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 216..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 268 AA; 29262 MW; 464EC059ADE51F0F CRC64;
MLRIAGRKLS SSAAARSSSA FFTRNPFTFT DDSSSPTRSP SPTSLASQFL DQFRGFSSNS
VSPAHQTGLV SDLPATVAAI KNPSSKIVYD DSNHERYPPG DPSKRAFAYF VLTGGRFVYA
SLVRLLILKF VLSMSASKDV LALASLEVDL SSIEPGTTVT VKWRGKPVFI RRRTDEDINL
ANSVDLGSLR DPQQDAERVK NPEWLVVIGV CTHLGCIPLP NAGDFGGWFC PCHGSHYDIS
GRIRKGPAPY NLEVPTYSFM EENKLLIG
