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Q9YHT2

- SDHB_CHICK

UniProt

Q9YHT2 - SDHB_CHICK

Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

SDHB

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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).

    Catalytic activityi

    Succinate + a quinone = fumarate + a quinol.

    Cofactori

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi103 – 1031Iron-sulfur 1 (2Fe-2S)
    Metal bindingi108 – 1081Iron-sulfur 1 (2Fe-2S)
    Metal bindingi111 – 1111Iron-sulfur 1 (2Fe-2S)
    Metal bindingi123 – 1231Iron-sulfur 1 (2Fe-2S)
    Metal bindingi196 – 1961Iron-sulfur 2 (4Fe-4S)
    Metal bindingi199 – 1991Iron-sulfur 2 (4Fe-4S)
    Metal bindingi202 – 2021Iron-sulfur 2 (4Fe-4S)
    Metal bindingi206 – 2061Iron-sulfur 3 (3Fe-4S)
    Binding sitei211 – 2111Ubiquinone; shared with DHSD2 Publications
    Metal bindingi253 – 2531Iron-sulfur 3 (3Fe-4S)
    Metal bindingi259 – 2591Iron-sulfur 3 (3Fe-4S)
    Metal bindingi263 – 2631Iron-sulfur 2 (4Fe-4S)

    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. small molecule metabolic process Source: Reactome
    2. tricarboxylic acid cycle Source: Reactome

    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_115536. The tricarboxylic acid 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
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Mitochondrion inner membrane 3 Publications; Peripheral membrane protein 3 Publications; Matrix side 3 Publications

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB
    2. 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
    Transit peptidei1 – 3838MitochondrionAdd
    BLAST
    Chaini39 – 290252Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000343800Add
    BLAST

    Proteomic databases

    PaxDbiQ9YHT2.
    PRIDEiQ9YHT2.

    Interactioni

    Subunit structurei

    Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD.3 Publications

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000000693.

    Structurei

    Secondary structure

    1
    290
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi49 – 568
    Beta strandi67 – 748
    Helixi75 – 773
    Helixi82 – 9211
    Beta strandi104 – 1085
    Beta strandi112 – 1154
    Beta strandi118 – 1214
    Helixi122 – 1243
    Beta strandi135 – 1384
    Beta strandi140 – 1423
    Beta strandi144 – 1474
    Helixi154 – 1629
    Turni173 – 1764
    Helixi184 – 1885
    Turni189 – 1957
    Helixi203 – 2053
    Helixi207 – 2126
    Turni213 – 2153
    Helixi218 – 22912
    Helixi237 – 2426
    Turni247 – 2526
    Helixi258 – 2625
    Helixi269 – 28214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YQ3X-ray2.20B39-290[»]
    1YQ4X-ray2.33B39-290[»]
    2FBWX-ray2.10B/O39-290[»]
    2H88X-ray1.74B/O39-290[»]
    2H89X-ray2.40B39-290[»]
    2WQYX-ray2.10B/O39-290[»]
    ProteinModelPortaliQ9YHT2.
    SMRiQ9YHT2. Positions 44-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9YHT2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 143942Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini186 – 216314Fe-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.
    HOVERGENiHBG005483.
    InParanoidiQ9YHT2.
    PhylomeDBiQ9YHT2.

    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.

    Q9YHT2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAVVGVSL RRGVPARFLR AGLRPVRGLE AVHGICRGAQ TAAAATSRIK    50
    KFSIYRWDPD KPGDKPRMQT YEVDLNKCGP MVLDALIKIK NELDSTLTFR 100
    RSCREGICGS CAMNIAGGNT LACTKKIDPD LSKTTKIYPL PHMYVVKDLV 150
    PDLSNFYAQY KSIEPYLKKK DESKQGKEQY LQSIEDRQKL DGLYECILCA 200
    CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDYTEER LAQLQDPFSL 250
    YRCHTIMNCT RTCPKGLNPG KAIAEIKKMM ATYKEKAAAA 290
    Length:290
    Mass (Da):32,597
    Last modified:May 1, 1999 - v1
    Checksum:i313E698866B3FDFC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095937 mRNA. Translation: AAC72372.1.
    UniGeneiGga.4743.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095937 mRNA. Translation: AAC72372.1 .
    UniGenei Gga.4743.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YQ3 X-ray 2.20 B 39-290 [» ]
    1YQ4 X-ray 2.33 B 39-290 [» ]
    2FBW X-ray 2.10 B/O 39-290 [» ]
    2H88 X-ray 1.74 B/O 39-290 [» ]
    2H89 X-ray 2.40 B 39-290 [» ]
    2WQY X-ray 2.10 B/O 39-290 [» ]
    ProteinModelPortali Q9YHT2.
    SMRi Q9YHT2. Positions 44-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000000693.

    Proteomic databases

    PaxDbi Q9YHT2.
    PRIDEi Q9YHT2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0479.
    HOGENOMi HOG000160590.
    HOVERGENi HBG005483.
    InParanoidi Q9YHT2.
    PhylomeDBi Q9YHT2.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01006 .
    Reactomei REACT_115536. The tricarboxylic acid cycle.

    Miscellaneous databases

    EvolutionaryTracei Q9YHT2.
    NextBioi 20920287.
    PROi Q9YHT2.

    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. "OXPHOS genes in mammals and the molecular clock."
      Weinreich D.M.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    2. "Crystallization of mitochondrial respiratory complex II from chicken heart: a membrane-protein complex diffracting to 2.0 A."
      Huang L.-S., Borders T.M., Shen J.T., Wang C.-J., Berry E.A.
      Acta Crystallogr. D 61:380-387(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OF 39-290, SUBUNIT, SUBCELLULAR LOCATION.
    3. "Crystallographic studies of the binding of ligands to the dicarboxylate site of complex II, and the identity of the ligand in the 'oxaloacetate-inhibited' state."
      Huang L.-S., Shen J.T., Wang A.C., Berry E.A.
      Biochim. Biophys. Acta 1757:1073-1083(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF OF 39-290 IN COMPLEX WITH UBIQUINONE AND IRON-SULFUR CENTERS, SUBUNIT, SUBCELLULAR LOCATION.
    4. "3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme."
      Huang L.-S., Sun G., Cobessi D., Wang A.C., Shen J.T., Tung E.Y., Anderson V.E., Berry E.A.
      J. Biol. Chem. 281:5965-5972(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 39-290 IN COMPLEX WITH UBIQUINONE AND IRON-SULFUR CENTERS, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiSDHB_CHICK
    AccessioniPrimary (citable) accession number: Q9YHT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3