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Q75CI4

- SDHB_ASHGO

UniProt

Q75CI4 - SDHB_ASHGO

Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

SDH2

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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 bindingi82 – 821Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi87 – 871Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi90 – 901Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi102 – 1021Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi174 – 1741Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi177 – 1771Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi180 – 1801Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi184 – 1841Iron-sulfur 3 (3Fe-4S)By similarity
    Binding sitei189 – 1891Ubiquinone; shared with DHSDBy similarity
    Metal bindingi231 – 2311Iron-sulfur 3 (3Fe-4S)By similarity
    Metal bindingi237 – 2371Iron-sulfur 3 (3Fe-4S)By similarity
    Metal bindingi241 – 2411Iron-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: UniProtKB-EC

    GO - Biological processi

    1. 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

    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
    Ordered Locus Names:ACL065C
    OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
    Taxonomic identifieri284811 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
    ProteomesiUP000000591: Chromosome III

    Subcellular locationi

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

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 261Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000010347
    Transit peptidei1 – ?Mitochondrion

    Proteomic databases

    PRIDEiQ75CI4.

    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

    STRINGi33169.AGOS_ACL065C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ75CI4.
    SMRiQ75CI4. Positions 24-259.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 122922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini164 – 194314Fe-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.
    OMAiDAAPFMQ.
    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.

    Q75CI4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVFRAGIGRI GLIRGLATQA AEVSATRYKS FKIYRWNPDT PAEKPRMQEY    50
    KVDLNKCGPM VLDALIKIKN EQDPTLTFRR SCREGICGSC AMNIGGRNTL 100
    ACLCKIDQAE NKDVKIYPLP HMYVVKDLVP DLTNFYKQYK SIQPYLQKAS 150
    KPADGREHLQ SIADRKKLDG LYECILCACC STACPSYWWN NEQYLGPAVL 200
    MQAYRWMVDS RDGAGAGRRE QLQNAMSVYR CHTIMNCTRT CPKGLNPGKA 250
    IAEIKKALAF A 261
    Length:261
    Mass (Da):29,436
    Last modified:July 5, 2004 - v1
    Checksum:i7F11084887FC7F5A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016816 Genomic DNA. Translation: AAS51163.1.
    RefSeqiNP_983339.1. NM_208692.1.

    Genome annotation databases

    EnsemblFungiiAAS51163; AAS51163; AGOS_ACL065C.
    GeneIDi4619459.
    KEGGiago:AGOS_ACL065C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016816 Genomic DNA. Translation: AAS51163.1 .
    RefSeqi NP_983339.1. NM_208692.1.

    3D structure databases

    ProteinModelPortali Q75CI4.
    SMRi Q75CI4. Positions 24-259.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 33169.AGOS_ACL065C.

    Proteomic databases

    PRIDEi Q75CI4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii AAS51163 ; AAS51163 ; AGOS_ACL065C .
    GeneIDi 4619459.
    KEGGi ago:AGOS_ACL065C.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01006 .

    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 Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
      Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
      Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
    2. "Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
      Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
      G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

    Entry informationi

    Entry nameiSDHB_ASHGO
    AccessioniPrimary (citable) accession number: Q75CI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3