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Q9N0F1

- ODO2_PIG

UniProt

Q9N0F1 - ODO2_PIG

Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene

DLST

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).1 Publication

    Catalytic activityi

    Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei426 – 4261Sequence Analysis
    Active sitei430 – 4301Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
    2. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    ReactomeiREACT_205223. Lysine catabolism.
    REACT_217226. Citric acid cycle (TCA cycle).
    UniPathwayiUPA00868; UER00840.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC:2.3.1.61)
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex component E2
    Short name:
    OGDC-E2
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
    E2K
    E2o
    Short name:
    PE2o
    Gene namesi
    Name:DLST
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 7

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. nucleus Source: Ensembl
    3. oxoglutarate dehydrogenase complex Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi374 – 3741S → A: Loss of activity. 1 Publication
    Mutagenesisi426 – 4261H → C: 16% of activity. 1 Publication
    Mutagenesisi430 – 4301D → A, E or N: Loss of activity. 1 Publication
    Mutagenesisi451 – 4533LLL → AAA or DDD: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6868MitochondrionAdd
    BLAST
    Chaini69 – 455387Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020474Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei111 – 1111N6-lipoyllysineSequence Analysis
    Modified residuei155 – 1551N6-acetyllysineBy similarity
    Modified residuei269 – 2691N6-acetyllysineBy similarity
    Modified residuei274 – 2741N6-acetyllysineBy similarity
    Modified residuei275 – 2751N6-acetyllysineBy similarity
    Modified residuei279 – 2791N6-acetyllysineBy similarity
    Modified residuei309 – 3091N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9N0F1.
    PRIDEiQ9N0F1.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9N0F1.
    SMRiQ9N0F1. Positions 222-455.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 14473Lipoyl-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni221 – 453233CatalyticAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi151 – 21565Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    GeneTreeiENSGT00740000115255.
    HOGENOMiHOG000281563.
    HOVERGENiHBG000268.
    KOiK00658.
    OMAiAEDEVIC.
    OrthoDBiEOG78PV93.
    TreeFamiTF314164.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    TIGRFAMsiTIGR01347. sucB. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9N0F1-1 [UniParc]FASTAAdd to Basket

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    MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGISLCQGP GYPDSRKIVI    50
    SNSSVLNVRF FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE 100
    DEVVCEIETD KTSVQVPSPA NGVIEALLVP DGGKVEGGTP LFTLRKTGAA 150
    PAKAKPAEAP AAAAPKAEPA VSAVPPPPAA SIPTQMPPVP SPPQPLTSKP 200
    VSAVKPTAAP PVAEPGAVKG LRAEHREKMN RMRQRIAQRL KEAQNTCAML 250
    TTFNEIDMSN IQDMRARHKE AFLKKHNLKL GFMSAFVKAS AFALQEQPVV 300
    NAVIDDTTKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS 350
    ELGEKARKNE LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA 400
    IVDRPVAVGG KVEIRPMMYV ALTYDHRLID GREAVTFLRK IKAAVEDPRV 450
    LLLDL 455
    Length:455
    Mass (Da):48,977
    Last modified:October 1, 2000 - v1
    Checksum:i563B5E7455C842FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB035206 mRNA. Translation: BAA95700.1.
    RefSeqiNP_999562.1. NM_214397.1.
    UniGeneiSsc.2730.

    Genome annotation databases

    EnsembliENSSSCT00000002639; ENSSSCP00000002572; ENSSSCG00000002374.
    GeneIDi397690.
    KEGGissc:397690.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB035206 mRNA. Translation: BAA95700.1 .
    RefSeqi NP_999562.1. NM_214397.1.
    UniGenei Ssc.2730.

    3D structure databases

    ProteinModelPortali Q9N0F1.
    SMRi Q9N0F1. Positions 222-455.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q9N0F1.
    PRIDEi Q9N0F1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000002639 ; ENSSSCP00000002572 ; ENSSSCG00000002374 .
    GeneIDi 397690.
    KEGGi ssc:397690.

    Organism-specific databases

    CTDi 1743.

    Phylogenomic databases

    eggNOGi COG0508.
    GeneTreei ENSGT00740000115255.
    HOGENOMi HOG000281563.
    HOVERGENi HBG000268.
    KOi K00658.
    OMAi AEDEVIC.
    OrthoDBi EOG78PV93.
    TreeFami TF314164.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .
    Reactomei REACT_205223. Lysine catabolism.
    REACT_217226. Citric acid cycle (TCA cycle).

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    TIGRFAMsi TIGR01347. sucB. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase complex."
      Koike K., Suematsu T., Ehara M.
      Eur. J. Biochem. 267:3005-3016(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS.
      Tissue: Brain cortex and Heart.

    Entry informationi

    Entry nameiODO2_PIG
    AccessioniPrimary (citable) accession number: Q9N0F1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 95 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

    Complete proteome, Direct protein sequencing, 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