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Database: UniProt
Entry: P21911
LinkDB: P21911
Original site: P21911 
ID   SDHB_SCHPO              Reviewed;         275 AA.
AC   P21911; P21915;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 3.
DT   16-JAN-2019, entry version 162.
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; ORFNames=SPAC140.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K.,
RA   Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.,
RA   Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L.,
RA   FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D.,
RA   Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M.,
RA   Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M.,
RA   Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D.,
RA   Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H.,
RA   Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-251.
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   [4]
RP   ERRATUM.
RA   Gould S.J., Subramani S., Scheffler I.E.;
RL   Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993).
CC   -!- FUNCTION: Iron-sulfur protein (IP) subunit of succinate
CC       dehydrogenase (SDH) that is involved in complex II of the
CC       mitochondrial electron transport chain and is responsible for
CC       transferring electrons from succinate to ubiquinone (coenzyme Q).
CC       {ECO:0000250}.
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: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 {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Matrix side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family. {ECO:0000305}.
DR   EMBL; CU329670; CAB86412.2; -; Genomic_DNA.
DR   PIR; D32394; D32394.
DR   PIR; T37633; T37633.
DR   RefSeq; NP_593530.2; NM_001018964.2.
DR   SMR; P21911; -.
DR   BioGrid; 279288; 2.
DR   ComplexPortal; CPX-566; Mitochondrial respiratory chain complex II.
DR   STRING; 4896.SPAC140.01.1; -.
DR   MaxQB; P21911; -.
DR   PaxDb; P21911; -.
DR   PRIDE; P21911; -.
DR   EnsemblFungi; SPAC140.01.1; SPAC140.01.1:pep; SPAC140.01.
DR   GeneID; 2542842; -.
DR   KEGG; spo:SPAC140.01; -.
DR   EuPathDB; FungiDB:SPAC140.01; -.
DR   PomBase; SPAC140.01; sdh2.
DR   HOGENOM; HOG000160590; -.
DR   InParanoid; P21911; -.
DR   KO; K00235; -.
DR   OMA; DGQYFGP; -.
DR   Reactome; R-SPO-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER01006.
DR   PRO; PR:P21911; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:PomBase.
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; ISS:PomBase.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:PomBase.
DR   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR   GO; GO:0006105; P:succinate metabolic process; ISS:PomBase.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:PomBase.
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   3: Inferred from homology;
KW   2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW   Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT       1     24       Mitochondrion. {ECO:0000255}.
FT   CHAIN        25    275       Succinate dehydrogenase [ubiquinone]
FT                                iron-sulfur subunit, mitochondrial.
FT                                /FTId=PRO_0000010350.
FT   DOMAIN       57    137       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      178    208       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        98     98       Iron-sulfur (2Fe-2S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   METAL       103    103       Iron-sulfur (2Fe-2S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   METAL       106    106       Iron-sulfur (2Fe-2S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   METAL       118    118       Iron-sulfur (2Fe-2S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   METAL       188    188       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       191    191       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       194    194       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       198    198       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       245    245       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       251    251       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       255    255       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   BINDING     203    203       Ubiquinone; shared with DHSD.
FT                                {ECO:0000250}.
SQ   SEQUENCE   275 AA;  31426 MW;  F44661005266A678 CRC64;
     MFSRRIQVLS PFLKHFVNRN ARMMATEANI SATSANPQSQ GENLKTFEIY RWNPEKPEVK
     PKLQKYTVDL TKCGPMVLDA LIKIKNEQDP TLTFRRSCRE GICGSCAMNI NGSNTLACIC
     NIKKDNKPTK IYPLPHCFIV KDLVPDLTYF YKQYKSIEPW LQNDNIPKDK EFYQSRADRA
     KLDGLYECIL CACCSTSCPS YWWNSEEYLG PAVLMQAYRW IIDSRDQATA KRLDVMQNSM
     SVYRCHTIMN CARTCPKGLN PGLAIAKVKA LMATA
//
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