SDHB_YEAST
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 03-AUG-2022, entry version 201.
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; 167.
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; P21801; -.
DR PRIDE; P21801; -.
DR EnsemblFungi; YLL041C_mRNA; YLL041C; YLL041C.
DR GeneID; 850685; -.
DR KEGG; sce:YLL041C; -.
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 BioCyc; MetaCyc:YLL041C-MON; -.
DR BioCyc; YEAST:YLL041C-MON; -.
DR Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER01006.
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: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; 1.10.1060.10; -; 1.
DR Gene3D; 3.10.20.30; -; 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 Pfam; PF13085; Fer2_3; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR00384; dhsB; 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
