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Database: UniProt/SWISS-PROT
Entry: SDHB_YEAST
LinkDB: SDHB_YEAST
Original site: 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   23-MAY-2018, entry version 177.
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;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2191948;
RA   Lombardo A., Carine K., Scheffler I.E.;
RT   "Cloning and characterization of the iron-sulfur subunit gene of
RT   succinate 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.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding 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:
RT   isolation of partial cDNA or genomic clones encoding the iron-sulfur
RT   protein of succinate dehydrogenase from several species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989).
RN   [6]
RP   ERRATUM.
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
RT   Saccharomyces 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.,
RA   Dephoure N., 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
RT   dynamics simulation studies.";
RL   J. Biol. Chem. 279:9424-9431(2004).
CC   -!- FUNCTION: Subunit of succinate dehydrogenase (SDH) that is
CC       involved in complex II of the mitochondrial electron transport
CC       chain and is responsible for transferring electrons from succinate
CC       to ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic
CC       dimer. Electrons flow from succinate to the FAD bound to SDH1, and
CC       sequentially through the iron-sulfur clusters bound to SDH2 and
CC       enter the membrane dimer formed by SDH3 and SDH4.
CC   -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate 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
CC       membrane protein; Matrix side.
CC   -!- MISCELLANEOUS: Present with 9540 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family. {ECO:0000305}.
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   PDB; 1ORZ; Model; -; B=21-266.
DR   PDB; 1PB4; Model; -; B=21-266.
DR   PDBsum; 1ORZ; -.
DR   PDBsum; 1PB4; -.
DR   ProteinModelPortal; P21801; -.
DR   SMR; P21801; -.
DR   BioGrid; 31272; 152.
DR   DIP; DIP-5856N; -.
DR   IntAct; P21801; 6.
DR   STRING; 4932.YLL041C; -.
DR   MaxQB; P21801; -.
DR   PaxDb; P21801; -.
DR   PRIDE; P21801; -.
DR   EnsemblFungi; YLL041C; YLL041C; YLL041C.
DR   GeneID; 850685; -.
DR   KEGG; sce:YLL041C; -.
DR   EuPathDB; FungiDB:YLL041C; -.
DR   SGD; S000003964; SDH2.
DR   GeneTree; ENSGT00390000013558; -.
DR   HOGENOM; HOG000160590; -.
DR   InParanoid; P21801; -.
DR   KO; K00235; -.
DR   OMA; DGQYFGP; -.
DR   OrthoDB; EOG092C401C; -.
DR   BioCyc; MetaCyc:YLL041C-MONOMER; -.
DR   BioCyc; YEAST:YLL041C-MONOMER; -.
DR   UniPathway; UPA00223; UER01006.
DR   PRO; PR:P21801; -.
DR   Proteomes; UP000002311; Chromosome XII.
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: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:0045333; P:cellular respiration; IMP:SGD.
DR   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IMP:SGD.
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; SSF46548; SSF46548; 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; 3D-structure; 3Fe-4S; 4Fe-4S; Complete proteome;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1    ?20       Mitochondrion.
FT   CHAIN       ?21    266       Succinate dehydrogenase [ubiquinone]
FT                                iron-sulfur subunit, mitochondrial.
FT                                /FTId=PRO_0000010353.
FT   DOMAIN       36    127       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      169    199       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        87     87       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        92     92       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        95     95       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       107    107       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       179    179       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       182    182       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       185    185       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       189    189       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       236    236       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       242    242       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       246    246       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   BINDING     194    194       Ubiquinone; shared with DHSD.
FT                                {ECO:0000250}.
FT   MUTAGEN     260    266       Missing: Abolishes SDH activity and
FT                                complex assembly.
FT                                {ECO:0000269|PubMed:1390628}.
FT   MUTAGEN     260    260       K->T: Abolishes SDH activity. No effect
FT                                on complex assembly and stability; when
FT                                associated with T-261.
FT                                {ECO:0000269|PubMed:1390628}.
FT   MUTAGEN     261    261       K->T: Abolishes SDH activity. No effect
FT                                on complex assembly and stability; when
FT                                associated with T-260.
FT                                {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
//
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