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P21911

- SDHB_SCHPO

UniProt

P21911 - SDHB_SCHPO

Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

sdh2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (13 Jun 2012)
      Previous versions | rss
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    Functioni

    Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).By similarity

    Catalytic activityi

    Succinate + a quinone = fumarate + a quinol.

    Cofactori

    Binds 1 2Fe-2S cluster.By similarity
    Binds 1 3Fe-4S cluster.By similarity
    Binds 1 4Fe-4S cluster.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi98 – 981Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
    Metal bindingi103 – 1031Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
    Metal bindingi106 – 1061Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
    Metal bindingi118 – 1181Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
    Metal bindingi188 – 1881Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi191 – 1911Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi194 – 1941Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi198 – 1981Iron-sulfur 3 (3Fe-4S)By similarity
    Binding sitei203 – 2031Ubiquinone; shared with DHSDBy similarity
    Metal bindingi245 – 2451Iron-sulfur 3 (3Fe-4S)By similarity
    Metal bindingi251 – 2511Iron-sulfur 3 (3Fe-4S)By similarity
    Metal bindingi255 – 2551Iron-sulfur 2 (4Fe-4S)By similarity

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
    2. 3 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    3. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    4. electron carrier activity Source: InterPro
    5. metal ion binding Source: UniProtKB-KW
    6. succinate dehydrogenase (ubiquinone) activity Source: PomBase

    GO - Biological processi

    1. mitochondrial electron transport, succinate to ubiquinone Source: PomBase
    2. succinate metabolic process Source: PomBase
    3. tricarboxylic acid cycle Source: PomBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport, Tricarboxylic acid cycle

    Keywords - Ligandi

    2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_213505. Citric acid cycle (TCA cycle).
    UniPathwayiUPA00223; UER01006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC:1.3.5.1)
    Alternative name(s):
    Iron-sulfur subunit of complex II
    Short name:
    Ip
    Gene namesi
    Name:sdh2
    ORF Names:SPAC140.01
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC140.01.

    Subcellular locationi

    Mitochondrion inner membrane By similarity; Peripheral membrane protein By similarity; Matrix side By similarity

    GO - Cellular componenti

    1. cytoplasm Source: PomBase
    2. mitochondrial respiratory chain complex II Source: PomBase

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2424MitochondrionSequence AnalysisAdd
    BLAST
    Chaini25 – 275251Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000010350Add
    BLAST

    Proteomic databases

    MaxQBiP21911.
    PaxDbiP21911.

    Interactioni

    Subunit structurei

    Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit.By similarity

    Protein-protein interaction databases

    BioGridi279288. 2 interactions.
    MINTiMINT-4687642.
    STRINGi4896.SPAC140.01-1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 137812Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini178 – 208314Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
    Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0479.
    HOGENOMiHOG000160590.
    KOiK00235.
    OrthoDBiEOG7X9GJ0.

    Family and domain databases

    Gene3Di3.10.20.30. 1 hit.
    InterProiIPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    IPR017896. 4Fe4S_Fe-S-bd.
    IPR017900. 4Fe4S_Fe_S_CS.
    IPR012675. Beta-grasp_dom.
    IPR009051. Helical_ferredxn.
    IPR004489. Succ_DH/fum_Rdtase_Fe-S.
    IPR025192. Succ_DH/fum_Rdtase_N.
    [Graphical view]
    PfamiPF13085. Fer2_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF46548. SSF46548. 1 hit.
    SSF54292. SSF54292. 1 hit.
    TIGRFAMsiTIGR00384. dhsB. 1 hit.
    PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS00198. 4FE4S_FER_1. 1 hit.
    PS51379. 4FE4S_FER_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P21911-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFSRRIQVLS PFLKHFVNRN ARMMATEANI SATSANPQSQ GENLKTFEIY    50
    RWNPEKPEVK PKLQKYTVDL TKCGPMVLDA LIKIKNEQDP TLTFRRSCRE 100
    GICGSCAMNI NGSNTLACIC NIKKDNKPTK IYPLPHCFIV KDLVPDLTYF 150
    YKQYKSIEPW LQNDNIPKDK EFYQSRADRA KLDGLYECIL CACCSTSCPS 200
    YWWNSEEYLG PAVLMQAYRW IIDSRDQATA KRLDVMQNSM SVYRCHTIMN 250
    CARTCPKGLN PGLAIAKVKA LMATA 275
    Length:275
    Mass (Da):31,426
    Last modified:June 13, 2012 - v3
    Checksum:iF44661005266A678
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB86412.2.
    PIRiD32394.
    T37633.
    RefSeqiNP_593530.2. NM_001018964.2.

    Genome annotation databases

    EnsemblFungiiSPAC140.01.1; SPAC140.01.1:pep; SPAC140.01.
    GeneIDi2542842.
    KEGGispo:SPAC140.01.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB86412.2 .
    PIRi D32394.
    T37633.
    RefSeqi NP_593530.2. NM_001018964.2.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 279288. 2 interactions.
    MINTi MINT-4687642.
    STRINGi 4896.SPAC140.01-1.

    Proteomic databases

    MaxQBi P21911.
    PaxDbi P21911.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC140.01.1 ; SPAC140.01.1:pep ; SPAC140.01 .
    GeneIDi 2542842.
    KEGGi spo:SPAC140.01.

    Organism-specific databases

    PomBasei SPAC140.01.

    Phylogenomic databases

    eggNOGi COG0479.
    HOGENOMi HOG000160590.
    KOi K00235.
    OrthoDBi EOG7X9GJ0.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01006 .
    Reactomei REACT_213505. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    NextBioi 20803883.
    PROi P21911.

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    InterProi IPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    IPR017896. 4Fe4S_Fe-S-bd.
    IPR017900. 4Fe4S_Fe_S_CS.
    IPR012675. Beta-grasp_dom.
    IPR009051. Helical_ferredxn.
    IPR004489. Succ_DH/fum_Rdtase_Fe-S.
    IPR025192. Succ_DH/fum_Rdtase_N.
    [Graphical view ]
    Pfami PF13085. Fer2_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46548. SSF46548. 1 hit.
    SSF54292. SSF54292. 1 hit.
    TIGRFAMsi TIGR00384. dhsB. 1 hit.
    PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS00198. 4FE4S_FER_1. 1 hit.
    PS51379. 4FE4S_FER_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "Comparative functional genomics of the fission yeasts."
      Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
      , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
      Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVISION OF GENE MODEL.
    3. "Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species."
      Gould S.J., Subramani S., Scheffler I.E.
      Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-251.
    4. Erratum
      Gould S.J., Subramani S., Scheffler I.E.
      Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)

    Entry informationi

    Entry nameiSDHB_SCHPO
    AccessioniPrimary (citable) accession number: P21911
    Secondary accession number(s): P21915
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: June 13, 2012
    Last modified: October 1, 2014
    This is version 134 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3