ID   SDHB_YEAST              Reviewed;         266 AA.
AC   P21801; D6VXW5;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial;
DE            EC=1.3.5.1;
DE   AltName: Full=Iron-sulfur subunit of complex II;
DE            Short=Ip;
DE   Flags: Precursor;
GN   Name=SDH2; Synonyms=SDH, SDHB; OrderedLocusNames=YLL041C;
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=2191948; DOI=10.1016/s0021-9258(18)86962-9;
RA   Lombardo A., Carine K., Scheffler I.E.;
RT   "Cloning and characterization of the iron-sulfur subunit gene of succinate
RT   dehydrogenase from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 265:10419-10423(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-242.
RX   PubMed=2494655; DOI=10.1073/pnas.86.6.1934;
RA   Gould S.J., Subramani S., Scheffler I.E.;
RT   "Use of the DNA polymerase chain reaction for homology probing: isolation
RT   of partial cDNA or genomic clones encoding the iron-sulfur protein of
RT   succinate dehydrogenase from several species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989).
RN   [6]
RP   ERRATUM OF PUBMED:2494655.
RA   Gould S.J., Subramani S., Scheffler I.E.;
RL   Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993).
RN   [7]
RP   MUTAGENESIS OF LYS-260; LYS-261 AND 260-LYS--ALA-266.
RX   PubMed=1390628; DOI=10.1021/bi00151a008;
RA   Schmidt D.M., Saghbini M., Scheffler I.E.;
RT   "The C-terminus of the succinate dehydrogenase IP peptide of Saccharomyces
RT   cerevisiae is significant for assembly of complex II.";
RL   Biochemistry 31:8442-8448(1992).
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   3D-STRUCTURE MODELING OF 21-266.
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: Subunit of succinate dehydrogenase (SDH) that is involved in
CC       complex II of the mitochondrial electron transport chain and is
CC       responsible for transferring electrons from succinate to ubiquinone
CC       (coenzyme Q). SDH1 and SDH2 form the catalytic dimer. Electrons flow
CC       from succinate to the FAD bound to SDH1, and sequentially through the
CC       iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed
CC       by SDH3 and SDH4.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (eukaryal route): step 1/1.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: a
CC       flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
CC       composed of a large and a small subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC       protein; Matrix side.
CC   -!- MISCELLANEOUS: Present with 9540 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC       iron-sulfur protein family. {ECO:0000305}.
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DR   EMBL; J05487; AAA35021.1; -; Genomic_DNA.
DR   EMBL; Z73146; CAA97492.1; -; Genomic_DNA.
DR   EMBL; AY558189; AAS56515.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09281.1; -; Genomic_DNA.
DR   PIR; A35435; RDBYIS.
DR   RefSeq; NP_013059.1; NM_001181861.1.
DR   AlphaFoldDB; P21801; -.
DR   SMR; P21801; -.
DR   BioGRID; 31272; 178.
DR   ComplexPortal; CPX-565; Mitochondrial respiratory chain complex II.
DR   DIP; DIP-5856N; -.
DR   IntAct; P21801; 6.
DR   STRING; 4932.YLL041C; -.
DR   MaxQB; P21801; -.
DR   PaxDb; 4932-YLL041C; -.
DR   PeptideAtlas; P21801; -.
DR   EnsemblFungi; YLL041C_mRNA; YLL041C; YLL041C.
DR   GeneID; 850685; -.
DR   KEGG; sce:YLL041C; -.
DR   AGR; SGD:S000003964; -.
DR   SGD; S000003964; SDH2.
DR   VEuPathDB; FungiDB:YLL041C; -.
DR   eggNOG; KOG3049; Eukaryota.
DR   GeneTree; ENSGT00390000013558; -.
DR   HOGENOM; CLU_044838_0_2_1; -.
DR   InParanoid; P21801; -.
DR   OMA; DGQYFGP; -.
DR   OrthoDB; 119960at2759; -.
DR   BioCyc; MetaCyc:YLL041C-MONOMER; -.
DR   BioCyc; YEAST:YLL041C-MONOMER; -.
DR   Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER01006.
DR   BioGRID-ORCS; 850685; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P21801; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P21801; Protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:SGD.
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:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IDA:SGD.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
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:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:ComplexPortal.
DR   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IDA:ComplexPortal.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR   InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR   NCBIfam; TIGR00384; dhsB; 1.
DR   PANTHER; PTHR11921:SF29; SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
DR   Pfam; PF13085; Fer2_3; 1.
DR   Pfam; PF13534; Fer4_17; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT         1..?20
FT                   /note="Mitochondrion"
FT   CHAIN           ?21..266
FT                   /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT                   subunit, mitochondrial"
FT                   /id="PRO_0000010353"
FT   DOMAIN          36..127
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          169..199
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         87
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /ligand_note="ligand shared with DHSD"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         260..266
FT                   /note="Missing: Abolishes SDH activity and complex
FT                   assembly."
FT                   /evidence="ECO:0000269|PubMed:1390628"
FT   MUTAGEN         260
FT                   /note="K->T: Abolishes SDH activity. No effect on complex
FT                   assembly and stability; when associated with T-261."
FT                   /evidence="ECO:0000269|PubMed:1390628"
FT   MUTAGEN         261
FT                   /note="K->T: Abolishes SDH activity. No effect on complex
FT                   assembly and stability; when associated with T-260."
FT                   /evidence="ECO:0000269|PubMed:1390628"
SQ   SEQUENCE   266 AA;  30231 MW;  C14170F3670F6930 CRC64;
     MLNVLLRRKA FCLVTKKGMA TATTAAATHT PRLKTFKVYR WNPDEPSAKP HLQSYQVDLN
     DCGPMVLDAL LKIKDEQDST LTFRRSCREG ICGSCAMNIG GRNTLACICK IDQNESKQLK
     IYPLPHMFIV KDLVPDLTNF YQQYKSIQPY LQRSSFPKDG TEVLQSIEDR KKLDGLYECI
     LCACCSTSCP SYWWNQEQYL GPAVLMQAYR WLIDSRDQAT KTRKAMLNNS MSLYRCHTIM
     NCTRTCPKGL NPGLAIAEIK KSLAFA
//