SDH3_YEAST
ID SDH3_YEAST Reviewed; 198 AA.
AC P33421; D6VX55;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b subunit, mitochondrial;
DE Flags: Precursor;
GN Name=SDH3; Synonyms=CYB3; OrderedLocusNames=YKL141W; ORFNames=YKL4;
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].
RX PubMed=1574929; DOI=10.1002/yea.320080309;
RA Abraham P.R., Mulder A., Van'T Riet J., Planta R.J., Raue H.A.;
RT "Molecular cloning and physical analysis of an 8.2 kb segment of chromosome
RT XI of Saccharomyces cerevisiae reveals five tightly linked genes.";
RL Yeast 8:227-238(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 51-79.
RX PubMed=8195189; DOI=10.1016/s0021-9258(17)40702-2;
RA Daignan-Fornier B., Valens M., Lemire B.D., Bolotin-Fukuhara M.;
RT "Structure and regulation of SDH3, the yeast gene encoding the cytochrome
RT b560 subunit of respiratory complex II.";
RL J. Biol. Chem. 269:15469-15472(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 CHARACTERIZATION.
RX PubMed=8152421; DOI=10.1007/bf00283426;
RA Abraham P.R., Mulder A., Van'T Riet J., Raue H.A.;
RT "Characterization of the Saccharomyces cerevisiae nuclear gene CYB3
RT encoding a cytochrome b polypeptide of respiratory complex II.";
RL Mol. Gen. Genet. 242:708-716(1994).
RN [7]
RP MUTAGENESIS OF PHE-153; HIS-163 AND TRP-166.
RX PubMed=10446163; DOI=10.1074/jbc.274.34.23956;
RA Oyedotun K.S., Lemire B.D.;
RT "The Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase.
RT Identification of Sdh3p amino acid residues involved in ubiquinone
RT binding.";
RL J. Biol. Chem. 274:23956-23962(1999).
RN [8]
RP REVIEW ON SUCCINATE DEHYDROGENASE.
RX PubMed=11803020; DOI=10.1016/s0005-2728(01)00229-8;
RA Lemire B.D., Oyedotun K.S.;
RT "The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone
RT oxidoreductase.";
RL Biochim. Biophys. Acta 1553:102-116(2002).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP MUTAGENESIS OF HIS-96 AND HIS-156.
RX PubMed=14672930; DOI=10.1074/jbc.m311877200;
RA Oyedotun K.S., Yau P.F., Lemire B.D.;
RT "Identification of the heme axial ligands in the cytochrome b562 of the
RT Saccharomyces cerevisiae succinate dehydrogenase.";
RL J. Biol. Chem. 279:9432-9439(2004).
RN [11]
RP 3D-STRUCTURE MODELING OF 51-198.
RX PubMed=14672929; DOI=10.1074/jbc.m311876200;
RA Oyedotun K.S., Lemire B.D.;
RT "The quaternary structure of the Saccharomyces cerevisiae succinate
RT dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics
RT simulation studies.";
RL J. Biol. Chem. 279:9424-9431(2004).
CC -!- FUNCTION: Membrane-anchoring mono-heme cytochrome b subunit of
CC succinate dehydrogenase (SDH) that is involved in system II of the
CC mitochondrial electron transport chain and is responsible for
CC transferring electrons from succinate to ubiquinone (coenzyme Q). SDH3
CC and SDH4 form the membrane dimer that anchors the catalytic dimer
CC formed by SDH1 and SDH2 to the matrix surface of the mitochondrial
CC inner membrane. Electrons originating from the catalytic dimer enter
CC the membrane dimer for ubiquinone reduction.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=The heme is bound between the two transmembrane subunits.;
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC -!- SUBUNIT: Forms part of complex II containing four subunits: a
CC flavoprotein (FP), an iron-sulfur protein (IP) and a cytochrome b
CC composed of two integral membrane proteins.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
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DR EMBL; Z25464; CAA80957.1; -; Genomic_DNA.
DR EMBL; X73884; CAA52088.1; -; Genomic_DNA.
DR EMBL; Z28141; CAA81982.1; -; Genomic_DNA.
DR EMBL; AY693024; AAT93043.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09021.1; -; Genomic_DNA.
DR PIR; S37970; S37970.
DR RefSeq; NP_012781.1; NM_001179707.1.
DR PDB; 6LO8; EM; 3.83 A; C=1-198.
DR PDBsum; 6LO8; -.
DR AlphaFoldDB; P33421; -.
DR SMR; P33421; -.
DR BioGRID; 33995; 71.
DR ComplexPortal; CPX-565; Mitochondrial respiratory chain complex II.
DR DIP; DIP-5310N; -.
DR IntAct; P33421; 1.
DR STRING; 4932.YKL141W; -.
DR MoonProt; P33421; -.
DR MaxQB; P33421; -.
DR PaxDb; P33421; -.
DR PRIDE; P33421; -.
DR EnsemblFungi; YKL141W_mRNA; YKL141W; YKL141W.
DR GeneID; 853716; -.
DR KEGG; sce:YKL141W; -.
DR SGD; S000001624; SDH3.
DR VEuPathDB; FungiDB:YKL141W; -.
DR eggNOG; KOG0449; Eukaryota.
DR GeneTree; ENSGT00390000000566; -.
DR HOGENOM; CLU_094691_0_0_1; -.
DR InParanoid; P33421; -.
DR OMA; RISGCVM; -.
DR BioCyc; MetaCyc:YKL141W-MON; -.
DR BioCyc; YEAST:YKL141W-MON; -.
DR Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; -.
DR PRO; PR:P33421; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P33421; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IDA:SGD.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IMP:SGD.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IDA:ComplexPortal.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IMP:SGD.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:ComplexPortal.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:ComplexPortal.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR018495; Succ_DH_cyt_bsu_CS.
DR InterPro; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR PANTHER; PTHR10978; PTHR10978; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
DR PROSITE; PS01000; SDH_CYT_1; 1.
DR PROSITE; PS01001; SDH_CYT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Quinone; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8195189"
FT CHAIN 51..198
FT /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT subunit, mitochondrial"
FT /id="PRO_0000003638"
FT TOPO_DOM 51..99
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..139
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..175
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..198
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 93
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with second transmembrane
FT subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT MUTAGEN 96
FT /note="H->A,D: Decreases quinone reductase activity."
FT /evidence="ECO:0000269|PubMed:14672930"
FT MUTAGEN 153
FT /note="F->V: Decreases quinone reductase activity. Little
FT effect on complex assembly."
FT /evidence="ECO:0000269|PubMed:10446163"
FT MUTAGEN 156
FT /note="H->A: Decreases SDH cytochrome b content."
FT /evidence="ECO:0000269|PubMed:14672930"
FT MUTAGEN 163
FT /note="H->Q: Decreases quinone reductase activity. Little
FT effect on complex assembly."
FT /evidence="ECO:0000269|PubMed:10446163"
FT MUTAGEN 166
FT /note="W->R: Decreases quinone reductase activity. Little
FT effect on complex assembly."
FT /evidence="ECO:0000269|PubMed:10446163"
FT MUTAGEN 167
FT /note="D->V: Reduces SDH FAD content. Probably impairs
FT complex assembly."
FT CONFLICT 10
FT /note="L -> A (in Ref. 2; CAA52088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22068 MW; F210FE99AE97607A CRC64;
MSAMMVKLGL NKSALLLKPS AFSRAAALSS SRRLLFNTAR TNFLSTSPLK NVASEMNTKA
AIAEEQILNK QRAKRPISPH LTIYQPQLTW YLSSLHRISL VLMGLGFYLF TILFGVSGLL
GLGLTTEKVS NWYHQKFSKI TEWSIKGSFA YLFAIHYGGA IRHLIWDTAK ELTLKGVYRT
GYALIGFTAV LGTYLLTL
