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P21914

- SDHB_DROME

UniProt

P21914 - SDHB_DROME

Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

SdhB

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      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 bindingi100 – 1001Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi105 – 1051Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi108 – 1081Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi120 – 1201Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi195 – 1951Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi198 – 1981Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi201 – 2011Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi205 – 2051Iron-sulfur 3 (3Fe-4S)By similarity
    Binding sitei210 – 2101Ubiquinone; shared with DHSDBy similarity
    Metal bindingi252 – 2521Iron-sulfur 3 (3Fe-4S)By similarity
    Metal bindingi258 – 2581Iron-sulfur 3 (3Fe-4S)By similarity
    Metal bindingi262 – 2621Iron-sulfur 2 (4Fe-4S)By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. mitochondrial electron transport, succinate to ubiquinone Source: FlyBase
    2. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    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_207898. Respiratory electron transport.
    REACT_218888. 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:SdhB
    Synonyms:SDH
    ORF Names:CG3283
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0014028. SdhB.

    Subcellular locationi

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

    GO - Cellular componenti

    1. microtubule associated complex Source: FlyBase
    2. mitochondrial inner membrane Source: UniProtKB
    3. mitochondrial respiratory chain complex II Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 297Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000010357
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Proteomic databases

    PaxDbiP21914.

    Expressioni

    Tissue specificityi

    Most abundant in the adult thorax and low in abdominal tissues.1 Publication

    Developmental stagei

    Expressed throughout development; pupae have very low levels of expression, in contrast to larvae.1 Publication

    Gene expression databases

    BgeeiP21914.

    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

    BioGridi61486. 12 interactions.
    DIPiDIP-20115N.
    IntActiP21914. 3 interactions.
    MINTiMINT-929605.
    STRINGi7227.FBpp0085489.

    Structurei

    3D structure databases

    ProteinModelPortaliP21914.
    SMRiP21914. Positions 45-280.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 140942Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini185 – 215314Fe-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.
    GeneTreeiENSGT00390000013558.
    InParanoidiP21914.
    KOiK00235.
    OMAiSEPHWES.
    OrthoDBiEOG7H4DTN.
    PhylomeDBiP21914.

    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.

    P21914-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLATEARQIL SRVGSLVARN QMRAISNGTA QLEQQAQPKE AQEPQIKKFE    50
    IYRWNPDNAG EKPYMQTYEV DLRECGPMVL DALIKIKNEM DPTLTFRRSC 100
    REGICGSCAM NIGGTNTLAC ISKIDINTSK SLKVYPLPHM YVVRDLVPDM 150
    NNFYEQYRNI QPWLQRKNEA GEKKGKAQYL QSVEDRSKLD GLYECILCAC 200
    CSTSCPSYWW NAEKYLGPAV LMQAYRWIID SRDENSAERL NKLKDPFSVY 250
    RCHTIMNCTR TCPKGLNPGR AIAEIKKLLS GLASKPAPKL ETAALHK 297
    Length:297
    Mass (Da):33,741
    Last modified:February 1, 1995 - v2
    Checksum:i892380E8BAE08FFF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27705 Genomic DNA. Translation: AAA61925.1.
    AE013599 Genomic DNA. Translation: AAF57396.1.
    AY118923 mRNA. Translation: AAM50783.1.
    RefSeqiNP_477101.1. NM_057753.5.
    UniGeneiDm.497.

    Genome annotation databases

    EnsemblMetazoaiFBtr0086156; FBpp0085489; FBgn0014028.
    GeneIDi35590.
    KEGGidme:Dmel_CG3283.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27705 Genomic DNA. Translation: AAA61925.1 .
    AE013599 Genomic DNA. Translation: AAF57396.1 .
    AY118923 mRNA. Translation: AAM50783.1 .
    RefSeqi NP_477101.1. NM_057753.5.
    UniGenei Dm.497.

    3D structure databases

    ProteinModelPortali P21914.
    SMRi P21914. Positions 45-280.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 61486. 12 interactions.
    DIPi DIP-20115N.
    IntActi P21914. 3 interactions.
    MINTi MINT-929605.
    STRINGi 7227.FBpp0085489.

    Proteomic databases

    PaxDbi P21914.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0086156 ; FBpp0085489 ; FBgn0014028 .
    GeneIDi 35590.
    KEGGi dme:Dmel_CG3283.

    Organism-specific databases

    CTDi 6390.
    FlyBasei FBgn0014028. SdhB.

    Phylogenomic databases

    eggNOGi COG0479.
    GeneTreei ENSGT00390000013558.
    InParanoidi P21914.
    KOi K00235.
    OMAi SEPHWES.
    OrthoDBi EOG7H4DTN.
    PhylomeDBi P21914.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01006 .
    Reactomei REACT_207898. Respiratory electron transport.
    REACT_218888. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    GenomeRNAii 35590.
    NextBioi 794181.
    PROi P21914.

    Gene expression databases

    Bgeei P21914.

    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. "Characterization of the gene encoding the iron-sulfur protein subunit of succinate dehydrogenase from Drosophila melanogaster."
      Au H.C., Scheffler I.E.
      Gene 149:261-265(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. "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: PRELIMINARY NUCLEOTIDE SEQUENCE OF 113-258.
    6. Erratum
      Gould S.J., Subramani S., Scheffler I.E.
      Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)

    Entry informationi

    Entry nameiSDHB_DROME
    AccessioniPrimary (citable) accession number: P21914
    Secondary accession number(s): Q9V9A0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3