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Q9YHT1

- SDHA_CHICK

UniProt

Q9YHT1 - SDHA_CHICK

Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene

SDHA

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      Previous versions | rss
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    Functioni

    Flavoprotein (FP) 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

    FAD.

    Enzyme regulationi

    Inhibited by oxaloacetate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei276 – 2761FAD1 Publication
    Binding sitei297 – 2971Substrate
    Binding sitei309 – 3091Substrate
    Active sitei341 – 3411Proton acceptor1 Publication
    Binding sitei408 – 4081Substrate
    Binding sitei441 – 4411FAD1 Publication
    Binding sitei452 – 4521Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi69 – 746FAD1 Publication
    Nucleotide bindingi92 – 10716FAD1 PublicationAdd
    BLAST
    Nucleotide bindingi457 – 4582FAD1 Publication

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

    GO - Biological processi

    1. respiratory electron transport chain Source: UniProtKB
    2. small molecule metabolic process Source: Reactome
    3. succinate metabolic process Source: UniProtKB
    4. tricarboxylic acid cycle Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport, Tricarboxylic acid cycle

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_115536. The tricarboxylic acid cycle.
    UniPathwayiUPA00223; UER01006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC:1.3.5.1)
    Alternative name(s):
    Flavoprotein subunit of complex II
    Short name:
    Fp
    Gene namesi
    Name:SDHA
    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 – 4444MitochondrionAdd
    BLAST
    Chaini45 – 665621Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialPRO_0000344984Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei100 – 1001Tele-8alpha-FAD histidine

    Proteomic databases

    PaxDbiQ9YHT1.
    PRIDEiQ9YHT1.

    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. Interacts with SDHAF2/SDH5; interaction is required for FAD attachment By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000021475.

    Structurei

    Secondary structure

    1
    665
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi58 – 6811
    Helixi72 – 8312
    Beta strandi88 – 947
    Helixi96 – 983
    Helixi100 – 1034
    Beta strandi114 – 1163
    Helixi120 – 13011
    Turni131 – 1333
    Helixi137 – 15620
    Beta strandi167 – 1693
    Beta strandi171 – 1799
    Turni180 – 1834
    Beta strandi186 – 1916
    Helixi197 – 20913
    Beta strandi215 – 2184
    Beta strandi220 – 2289
    Beta strandi231 – 2399
    Turni240 – 2423
    Beta strandi245 – 25511
    Helixi261 – 2633
    Beta strandi264 – 2696
    Helixi276 – 2838
    Beta strandi294 – 3018
    Turni302 – 3043
    Helixi311 – 3144
    Beta strandi318 – 3203
    Helixi328 – 3314
    Turni333 – 3353
    Helixi336 – 3383
    Helixi341 – 35313
    Turni354 – 3563
    Turni359 – 3624
    Beta strandi364 – 3685
    Helixi374 – 3807
    Helixi382 – 39211
    Turni396 – 3983
    Beta strandi401 – 41111
    Beta strandi413 – 4164
    Beta strandi420 – 4267
    Beta strandi429 – 43810
    Helixi440 – 4423
    Beta strandi446 – 4483
    Helixi457 – 47519
    Turni487 – 4904
    Helixi491 – 50111
    Beta strandi504 – 5085
    Helixi509 – 52315
    Beta strandi524 – 5285
    Helixi530 – 54516
    Helixi546 – 5494
    Helixi561 – 58525
    Beta strandi595 – 5984
    Helixi619 – 6213
    Beta strandi625 – 6328
    Turni633 – 6364
    Beta strandi637 – 6448
    Turni652 – 6543

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YQ3X-ray2.20A45-665[»]
    1YQ4X-ray2.33A45-665[»]
    2FBWX-ray2.10A/N45-665[»]
    2H88X-ray1.74A/N45-665[»]
    2H89X-ray2.40A45-665[»]
    2WQYX-ray2.10A/N45-665[»]
    ProteinModelPortaliQ9YHT1.
    SMRiQ9YHT1. Positions 52-665.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9YHT1.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1053.
    HOGENOMiHOG000160475.
    HOVERGENiHBG001461.
    InParanoidiQ9YHT1.
    KOiK00234.
    PhylomeDBiQ9YHT1.

    Family and domain databases

    Gene3Di1.20.58.100. 1 hit.
    3.90.700.10. 1 hit.
    InterProiIPR003953. FAD_bind_dom.
    IPR003952. FRD_SDH_FAD_BS.
    IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
    IPR027477. Succ_DH/fumarate_Rdtase_cat.
    IPR011281. Succ_DH_flav_su_fwd.
    IPR014006. Succ_Dhase_FrdA_Gneg.
    [Graphical view]
    PfamiPF00890. FAD_binding_2. 1 hit.
    PF02910. Succ_DH_flav_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF46977. SSF46977. 1 hit.
    SSF56425. SSF56425. 1 hit.
    TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
    TIGR01812. sdhA_frdA_Gneg. 1 hit.
    PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9YHT1-1 [UniParc]FASTAAdd to Basket

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    MAAVVAASRS LAKCWLRPAV RAWPAACQTH ARNFHFTVDG KKNASTKVSD    50
    SISTQYPVVD HEFDAVVVGA GGAGLRAAFG LSEAGFNTAC VTKLFPTRSH 100
    TVAAQGGINA ALGNMEDDNW RWHFYDTVKG SDWLGDQDAI HYMTEQAPAA 150
    VIELENYGMP FSRTEEGKIY QRAFGGQSLQ FGKGGQAHRC CCVADRTGHS 200
    LLHTLYGRSL RYDTSYFVEY FALDLLMENG ECRGVIALCI EDGTIHRFRA 250
    KNTVIATGGY GRTYFSCTSA HTSTGDGTAM VTRAGLPCQD LEFVQFHPTG 300
    IYGAGCLITE GCRGEGGILI NSQGERFMER YAPVAKDLAS RDVVSRSMTI 350
    EIREGRGCGP EKDHVYLQLH HLPPQQLATR LPGISETAMI FAGVDVTKEP 400
    IPVLPTVHYN MGGIPTNYKG QVITHVNGED KVVPGLYACG EAASASVHGA 450
    NRLGANSLLD LVVFGRACAL TIAETCKPGE PVPSIKPNAG EESVANLDKL 500
    RFADGTIRTS EARLNMQKTM QSHAAVFRTG SILQEGCEKL SQIYCDLAHL 550
    KTFDRGIVWN TDLVETLELQ NLMLCALQTI YGAEARKESR GAHAREDYKF 600
    RIDDFDYSKP LQGQQKRPFE EHWRKHTLSY VDVKSGKVTL KYRPVIDRTL 650
    NEEDCSSVPP AIRSY 665
    Length:665
    Mass (Da):72,931
    Last modified:July 22, 2008 - v2
    Checksum:i9476AA19A7A3AE84
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CO635738 mRNA. No translation available.
    AF095939 mRNA. Translation: AAC72374.1.
    RefSeqiNP_001264327.1. NM_001277398.1.
    UniGeneiGga.993.

    Genome annotation databases

    GeneIDi395758.
    KEGGigga:395758.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CO635738 mRNA. No translation available.
    AF095939 mRNA. Translation: AAC72374.1 .
    RefSeqi NP_001264327.1. NM_001277398.1.
    UniGenei Gga.993.

    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 A 45-665 [» ]
    1YQ4 X-ray 2.33 A 45-665 [» ]
    2FBW X-ray 2.10 A/N 45-665 [» ]
    2H88 X-ray 1.74 A/N 45-665 [» ]
    2H89 X-ray 2.40 A 45-665 [» ]
    2WQY X-ray 2.10 A/N 45-665 [» ]
    ProteinModelPortali Q9YHT1.
    SMRi Q9YHT1. Positions 52-665.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000021475.

    Proteomic databases

    PaxDbi Q9YHT1.
    PRIDEi Q9YHT1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 395758.
    KEGGi gga:395758.

    Organism-specific databases

    CTDi 6389.

    Phylogenomic databases

    eggNOGi COG1053.
    HOGENOMi HOG000160475.
    HOVERGENi HBG001461.
    InParanoidi Q9YHT1.
    KOi K00234.
    PhylomeDBi Q9YHT1.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei Q9YHT1.
    PROi Q9YHT1.

    Family and domain databases

    Gene3Di 1.20.58.100. 1 hit.
    3.90.700.10. 1 hit.
    InterProi IPR003953. FAD_bind_dom.
    IPR003952. FRD_SDH_FAD_BS.
    IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
    IPR027477. Succ_DH/fumarate_Rdtase_cat.
    IPR011281. Succ_DH_flav_su_fwd.
    IPR014006. Succ_Dhase_FrdA_Gneg.
    [Graphical view ]
    Pfami PF00890. FAD_binding_2. 1 hit.
    PF02910. Succ_DH_flav_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46977. SSF46977. 1 hit.
    SSF56425. SSF56425. 1 hit.
    TIGRFAMsi TIGR01816. sdhA_forward. 1 hit.
    TIGR01812. sdhA_frdA_Gneg. 1 hit.
    PROSITEi PS00504. FRD_SDH_FAD_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Detection of sequence polymorphisms in red junglefowl and white leghorn ESTs."
      Fitzsimmons C.J., Savolainen P., Amini B., Hjaelm G., Lundeberg J., Andersson L.
      Anim. Genet. 35:391-396(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-324.
    2. "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] OF 167-665.
      Tissue: Heart.
    3. "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 45-665 IN COMPLEX WITH FAD, SUBUNIT, SUBCELLULAR LOCATION.
    4. "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 45-665 IN COMPLEXES WITH FAD AND MALONATE, SUBUNIT, SUBCELLULAR LOCATION.
    5. "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 45-665 IN COMPLEXES WITH FAD; OXALOACETATE AND 3-NITROPROPIONIC ACID, ACTIVE SITE, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiSDHA_CHICK
    AccessioniPrimary (citable) accession number: Q9YHT1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 86 of the entry and version 2 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