UCRI_YEAST
ID UCRI_YEAST Reviewed; 215 AA.
AC P08067; D3DLM4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial;
DE EC=7.1.1.8 {ECO:0000269|PubMed:1657998, ECO:0000269|PubMed:2538628};
DE AltName: Full=Complex III subunit 5;
DE AltName: Full=Rieske iron-sulfur protein;
DE Short=RISP;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit;
DE Flags: Precursor;
GN Name=RIP1; OrderedLocusNames=YEL024W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-40.
RC STRAIN=ATCC 64665 / S288c / DC5;
RX PubMed=3036836; DOI=10.1016/s0021-9258(18)47500-x;
RA Beckmann J.D., Ljungdahl P.O., Lopez J.L., Trumpower B.L.;
RT "Isolation and characterization of the nuclear gene encoding the Rieske
RT iron-sulfur protein (RIP1) from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 262:8901-8909(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS, AND MUTAGENESIS OF PRO-203.
RX PubMed=2645276; DOI=10.1016/s0021-9258(19)84909-8;
RA Beckmann J.D., Ljungdahl P.O., Trumpower B.L.;
RT "Mutational analysis of the mitochondrial Rieske iron-sulfur protein of
RT Saccharomyces cerevisiae. I. Construction of a RIP1 deletion strain and
RT isolation of temperature-sensitive mutants.";
RL J. Biol. Chem. 264:3713-3722(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=8206223; DOI=10.1042/bst0220188;
RA Graham L.A., Brandt U., Trumpower B.L.;
RT "Protease maturation of the Rieske iron-sulphur protein after its insertion
RT into the mitochondrial cytochrome bc1 complex of Saccharomyces
RT cerevisiae.";
RL Biochem. Soc. Trans. 22:188-191(1994).
RN [7]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=6309810; DOI=10.1016/s0021-9258(17)44506-6;
RA Sidhu A., Beattie D.S.;
RT "Kinetics of assembly of complex III into the yeast mitochondrial membrane.
RT Evidence for a precursor to the iron-sulfur protein.";
RL J. Biol. Chem. 258:10649-10656(1983).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF GLY-157; GLY-163;
RP PRO-166; CYS-178; PRO-179; SER-183; ASP-186; GLY-189; PRO-195; ALA-196 AND
RP PRO-203.
RC STRAIN=D273-10B/A1;
RX PubMed=2538628; DOI=10.1016/0022-2836(89)90352-5;
RA Gatti D.L., Meinhardt S.W., Ohnishi T., Tzagoloff A.;
RT "Structure and function of the mitochondrial bc1 complex. A mutational
RT analysis of the yeast Rieske iron-sulfur protein.";
RL J. Mol. Biol. 205:421-435(1989).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF CYS-159; HIS-161;
RP CYS-164; CYS-178; HIS-181 AND HIS-184.
RX PubMed=1657998; DOI=10.1016/s0021-9258(18)54598-1;
RA Graham L.A., Trumpower B.L.;
RT "Mutational analysis of the mitochondrial Rieske iron-sulfur protein of
RT Saccharomyces cerevisiae. III. Import, protease processing, and assembly
RT into the cytochrome bc1 complex of iron-sulfur protein lacking the iron-
RT sulfur cluster.";
RL J. Biol. Chem. 266:22485-22492(1991).
RN [10]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10775262; DOI=10.1093/emboj/19.8.1777;
RA Schaegger H., Pfeiffer K.;
RT "Supercomplexes in the respiratory chains of yeast and mammalian
RT mitochondria.";
RL EMBO J. 19:1777-1783(2000).
RN [11]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10764779; DOI=10.1074/jbc.m001901200;
RA Cruciat C.M., Brunner S., Baumann F., Neupert W., Stuart R.A.;
RT "The cytochrome bc1 and cytochrome c oxidase complexes associate to form a
RT single supracomplex in yeast mitochondria.";
RL J. Biol. Chem. 275:18093-18098(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 31-215 IN COMPLEX WITH
RP IRON-SULFUR (2FE-2S), AND DISULFIDE BONDS.
RX PubMed=10873857; DOI=10.1016/s0969-2126(00)00152-0;
RA Hunte C., Koepke J., Lange C., Rossmanith T., Michel H.;
RT "Structure at 2.3 A resolution of the cytochrome bc1 complex from the yeast
RT Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment.";
RL Structure 8:669-684(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) OF 31-215 IN COMPLEX WITH
RP IRON-SULFUR (2FE-2S), AND DISULFIDE BONDS.
RX PubMed=11880631; DOI=10.1073/pnas.052704699;
RA Lange C., Hunte C.;
RT "Crystal structure of the yeast cytochrome bc1 complex with its bound
RT substrate cytochrome c.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-215 IN THE BC1 COMPLEX, COMPLEX
RP WITH IRON-SULFUR (2FE-2S), DISULFIDE BOND, AND SUBCELLULAR LOCATION.
RX PubMed=18390544; DOI=10.1074/jbc.m710126200;
RA Solmaz S.R., Hunte C.;
RT "Structure of complex III with bound cytochrome c in reduced state and
RT definition of a minimal core interface for electron transfer.";
RL J. Biol. Chem. 283:17542-17549(2008).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.23 ANGSTROMS).
RX PubMed=30598556; DOI=10.1038/s41594-018-0169-7;
RA Rathore S., Berndtsson J., Marin-Buera L., Conrad J., Carroni M.,
RA Brzezinski P., Ott M.;
RT "Cryo-EM structure of the yeast respiratory supercomplex.";
RL Nat. Struct. Mol. Biol. 26:50-57(2019).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS) IN COMPLEX WITH
RP IRON-SULFUR (2FE-2S).
RX PubMed=30598554; DOI=10.1038/s41594-018-0172-z;
RA Hartley A.M., Lukoyanova N., Zhang Y., Cabrera-Orefice A., Arnold S.,
RA Meunier B., Pinotsis N., Marechal A.;
RT "Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome
RT bc1.";
RL Nat. Struct. Mol. Biol. 26:78-83(2019).
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 (Probable). The Rieske protein is a catalytic
CC core subunit containing a [2Fe-2S] iron-sulfur cluster
CC (PubMed:18390544). It cycles between 2 conformational states during
CC catalysis to transfer electrons from the quinol bound in the Q(0) site
CC in cytochrome b (COB) to cytochrome c1 (CYT1) (PubMed:1657998,
CC PubMed:2538628) (Probable). {ECO:0000269|PubMed:1657998,
CC ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:2538628,
CC ECO:0000305|PubMed:11880631, ECO:0000305|PubMed:30598556}.
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; Evidence={ECO:0000269|PubMed:1657998,
CC ECO:0000269|PubMed:2538628};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
CC ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
CC ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 10 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein
CC (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular
CC weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10
CC (PubMed:1657998, PubMed:2538628, PubMed:10873857, PubMed:11880631,
CC PubMed:18390544, PubMed:30598554). The complex exists as an obligatory
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with a monomer or a dimer of cytochrome c oxidase (complex IV,
CC CIV), resulting in 2 different assemblies (supercomplexes III(2)IV and
CC III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556,
CC PubMed:30598554). RIP1 interacts with QCR10 on the intermembrane space
CC (IMS) side, and with QCR9 (PubMed:30598556, PubMed:30598554).
CC {ECO:0000269|PubMed:10764779, ECO:0000269|PubMed:10775262,
CC ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
CC ECO:0000269|PubMed:1657998, ECO:0000269|PubMed:18390544,
CC ECO:0000269|PubMed:2538628, ECO:0000269|PubMed:30598554,
CC ECO:0000269|PubMed:30598556}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass
CC membrane protein {ECO:0000269|PubMed:18390544,
CC ECO:0000269|PubMed:30598554}.
CC -!- PTM: Processed by both the mitochondrial processing peptidase (MPP) and
CC the mitochondrial intermediate protease (MIP). Initially, MPP removes
CC 22 amino acids from the newly imported precursor in the mitochondrial
CC matrix. This proteolytic processing is then followed by a second
CC proteolytic cleavage by MIP, which removes an octapeptide to generate
CC mature-sized RIP1. {ECO:0000269|PubMed:6309810,
CC ECO:0000269|PubMed:8206223}.
CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC {ECO:0000305|PubMed:18390544}.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M23316; AAA34980.1; -; Genomic_DNA.
DR EMBL; M24500; AAA34981.1; -; Genomic_DNA.
DR EMBL; U18530; AAB64501.1; -; Genomic_DNA.
DR EMBL; AY558341; AAS56667.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07628.1; -; Genomic_DNA.
DR PIR; A29318; A29318.
DR RefSeq; NP_010890.3; NM_001178839.3.
DR PDB; 1EZV; X-ray; 2.30 A; E=31-215.
DR PDB; 1KB9; X-ray; 2.30 A; E=31-215.
DR PDB; 1KYO; X-ray; 2.97 A; E/P=31-215.
DR PDB; 1P84; X-ray; 2.50 A; E=31-215.
DR PDB; 2IBZ; X-ray; 2.30 A; E=31-215.
DR PDB; 3CX5; X-ray; 1.90 A; E/P=31-215.
DR PDB; 3CXH; X-ray; 2.50 A; E/P=31-215.
DR PDB; 4PD4; X-ray; 3.04 A; E=31-215.
DR PDB; 6GIQ; EM; 3.23 A; E/P=1-215.
DR PDB; 6HU9; EM; 3.35 A; E/P=31-215.
DR PDB; 6T0B; EM; 2.80 A; E/P=31-215.
DR PDB; 6T15; EM; 3.29 A; E/P=31-215.
DR PDB; 6YMX; EM; 3.17 A; E/P=31-215.
DR PDBsum; 1EZV; -.
DR PDBsum; 1KB9; -.
DR PDBsum; 1KYO; -.
DR PDBsum; 1P84; -.
DR PDBsum; 2IBZ; -.
DR PDBsum; 3CX5; -.
DR PDBsum; 3CXH; -.
DR PDBsum; 4PD4; -.
DR PDBsum; 6GIQ; -.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR PDBsum; 6YMX; -.
DR AlphaFoldDB; P08067; -.
DR SMR; P08067; -.
DR BioGRID; 36705; 253.
DR ComplexPortal; CPX-567; Mitochondrial respiratory chain complex III.
DR DIP; DIP-6616N; -.
DR IntAct; P08067; 4.
DR STRING; 4932.YEL024W; -.
DR TCDB; 3.D.3.3.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR MaxQB; P08067; -.
DR PaxDb; P08067; -.
DR PRIDE; P08067; -.
DR ABCD; P08067; 1 sequenced antibody.
DR EnsemblFungi; YEL024W_mRNA; YEL024W; YEL024W.
DR GeneID; 856689; -.
DR KEGG; sce:YEL024W; -.
DR SGD; S000000750; RIP1.
DR VEuPathDB; FungiDB:YEL024W; -.
DR eggNOG; KOG1671; Eukaryota.
DR GeneTree; ENSGT00390000001014; -.
DR HOGENOM; CLU_055690_0_1_1; -.
DR InParanoid; P08067; -.
DR OMA; KRTWLIA; -.
DR BioCyc; MetaCyc:YEL024W-MON; -.
DR BioCyc; YEAST:YEL024W-MON; -.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR EvolutionaryTrace; P08067; -.
DR PRO; PR:P08067; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P08067; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IPI:SGD.
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; IMP:SGD.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR GO; GO:0045333; P:cellular respiration; IDA:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IDA:SGD.
DR DisProt; DP00687; -.
DR Gene3D; 1.20.5.270; -; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR037008; bc1_Rieske_TM_sf.
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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transit peptide; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:3036836,
FT ECO:0000269|PubMed:8206223"
FT PROPEP 23..30
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:3036836,
FT ECO:0000269|PubMed:8206223"
FT /id="PRO_0000449195"
FT CHAIN 31..215
FT /note="Cytochrome b-c1 complex subunit Rieske,
FT mitochondrial"
FT /id="PRO_0000030683"
FT TOPO_DOM 31..50
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554"
FT TRANSMEM 51..80
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554"
FT TOPO_DOM 81..215
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554"
FT DOMAIN 123..214
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 90..93
FT /note="Hinge"
FT /evidence="ECO:0000269|PubMed:30598556"
FT BINDING 159
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ,
FT ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH,
FT ECO:0007744|PDB:4PD4"
FT BINDING 161
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ,
FT ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH,
FT ECO:0007744|PDB:4PD4"
FT BINDING 178
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ,
FT ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH,
FT ECO:0007744|PDB:4PD4"
FT BINDING 181
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ,
FT ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH,
FT ECO:0007744|PDB:4PD4"
FT DISULFID 164..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
FT ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO,
FT ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ,
FT ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH,
FT ECO:0007744|PDB:4PD4"
FT MUTAGEN 157
FT /note="G->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2538628"
FT MUTAGEN 159
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1657998"
FT MUTAGEN 161
FT /note="H->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1657998"
FT MUTAGEN 163
FT /note="G->D: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:2538628"
FT MUTAGEN 164
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1657998"
FT MUTAGEN 166
FT /note="P->L: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:2538628"
FT MUTAGEN 178
FT /note="C->S,Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1657998,
FT ECO:0000269|PubMed:2538628"
FT MUTAGEN 179
FT /note="P->L: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:2538628"
FT MUTAGEN 180
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1657998"
FT MUTAGEN 181
FT /note="H->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1657998"
FT MUTAGEN 183
FT /note="S->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2538628"
FT MUTAGEN 184
FT /note="H->R: No loss of activity."
FT /evidence="ECO:0000269|PubMed:1657998"
FT MUTAGEN 186
FT /note="D->N: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:2538628"
FT MUTAGEN 189
FT /note="G->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2538628"
FT MUTAGEN 195
FT /note="P->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:2538628"
FT MUTAGEN 196
FT /note="A->T: No loss of activity."
FT /evidence="ECO:0000269|PubMed:2538628"
FT MUTAGEN 203
FT /note="P->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2538628,
FT ECO:0000269|PubMed:2645276"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6T0B"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1EZV"
FT HELIX 51..80
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6T15"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6T0B"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6YMX"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3CX5"
SQ SEQUENCE 215 AA; 23365 MW; 21981BD8492E86F3 CRC64;
MLGIRSSVKT CFKPMSLTSK RLISQSLLAS KSTYRTPNFD DVLKENNDAD KGRSYAYFMV
GAMGLLSSAG AKSTVETFIS SMTATADVLA MAKVEVNLAA IPLGKNVVVK WQGKPVFIRH
RTPHEIQEAN SVDMSALKDP QTDADRVKDP QWLIMLGICT HLGCVPIGEA GDFGGWFCPC
HGSHYDISGR IRKGPAPLNL EIPAYEFDGD KVIVG
