UCRI1_TOBAC
ID UCRI1_TOBAC Reviewed; 258 AA.
AC P49729;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Cytochrome b-c1 complex subunit Rieske-1, mitochondrial;
DE EC=7.1.1.8;
DE AltName: Full=Complex III subunit 5-1;
DE AltName: Full=Rieske iron-sulfur protein 1;
DE Short=RISP1;
DE AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit 1;
DE Flags: Precursor; Fragment;
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 TISSUE=Leaf;
RX PubMed=1961737; DOI=10.1073/pnas.88.23.10716;
RA Huang J.T., Struck F., Matzinger D.F., Levings C.S. III;
RT "Functional analysis in yeast of cDNA coding for the mitochondrial Rieske
RT iron-sulfur protein of higher plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10716-10720(1991).
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 -!- 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; M77225; AAA34112.1; -; mRNA.
DR PIR; B41607; B41607.
DR AlphaFoldDB; P49729; -.
DR SMR; P49729; -.
DR STRING; 4097.P49729; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:AgBase.
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; IGI:AgBase.
DR GO; GO:0009060; P:aerobic respiration; IGI:AgBase.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IGI:AgBase.
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..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 47..258
FT /note="Cytochrome b-c1 complex subunit Rieske-1,
FT mitochondrial"
FT /id="PRO_0000030676"
FT TOPO_DOM 47..95
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 96..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..258
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT DOMAIN 161..256
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 201
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 203
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 220
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 223
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 206..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT NON_TER 1
SQ SEQUENCE 258 AA; 28192 MW; FDA51B570CCEDCAF CRC64;
WPVRSAAPSS SAFISANHFS SDDDSSSPRS ISPSLASVFL HHTRGFSSNS VSPAHDMGLV
PDLPPTVAAI KNPTSKIVYD EHNHERYPPG DPSKRAFAYF VLTGGRFVYA SLMRLLILKF
VLSMSASKDV LALASLEVDL SSIEPGTTVT VKWRGKPVFI RRRTEDDISL ANSVDLGSLR
DPQQDAERVK NPEWLVVIGV CTHLGCIPLP NAGDFGGWFC PCHGSHYDIS GRIRKGPAPY
NLEVPTYSFL EENKLLIG
