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Q01205

- ODO2_RAT

UniProt

Q01205 - ODO2_RAT

Protein

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

Gene

Dlst

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (12 Apr 2005)
      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).

    Catalytic activityi

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

    Cofactori

    Binds 1 lipoyl cofactor covalently.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei425 – 4251Sequence Analysis
    Active sitei429 – 4291Sequence Analysis

    GO - Molecular functioni

    1. chaperone binding Source: RGD
    2. dihydrolipoyllysine-residue succinyltransferase activity Source: RGD
    3. heat shock protein binding Source: RGD

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: RGD
    2. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
    3. NADH metabolic process Source: RGD
    4. tricarboxylic acid cycle Source: RGD

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BRENDAi2.3.1.61. 5301.
    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
    Gene namesi
    Name:Dlst
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi1359615. Dlst.

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: RGD
    2. mitochondrion Source: RGD
    3. oxoglutarate dehydrogenase complex Source: RGD
    4. plasma membrane Source: RGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6868Mitochondrion2 PublicationsAdd
    BLAST
    Chaini69 – 454386Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020475Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei111 – 1111N6-lipoyllysineSequence Analysis
    Modified residuei155 – 1551N6-acetyllysineBy similarity
    Modified residuei268 – 2681N6-acetyllysineBy similarity
    Modified residuei273 – 2731N6-acetyllysineBy similarity
    Modified residuei274 – 2741N6-acetyllysineBy similarity
    Modified residuei278 – 2781N6-acetyllysineBy similarity
    Modified residuei308 – 3081N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ01205.
    PRIDEiQ01205.

    PTM databases

    PhosphoSiteiQ01205.

    Expressioni

    Gene expression databases

    GenevestigatoriQ01205.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.

    Protein-protein interaction databases

    IntActiQ01205. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01205.
    SMRiQ01205. Positions 221-454.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 14473Lipoyl-bindingAdd
    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.
    HOGENOMiHOG000281563.
    HOVERGENiHBG000268.
    InParanoidiQ01205.
    KOiK00658.
    PhylomeDBiQ01205.

    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.

    Q01205-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPDSRKMVI    50
    NNSSVFSVRF FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE 100
    DEVVCEIETD KTSVQVPSPA NGIIEALLVP DGGKVEGGTP LFTLRKTGAA 150
    PAKAKPAEAP ATAYKAAPEA PAAPPPPVAP VPTQMPPVPS PSQPPSSKPV 200
    SAIKPTAAPP LAEAGAAKGL RSEHREKMNR MRQRIAQRLK EAQNTCAMLT 250
    TFNEVDMSNI QEMRARHKDA FLKKHNLKLG FMSAFVKASA FALQEQPVVN 300
    AVIDDATKEV VYRDYIDISV AVATPRGLVV PVIRNVETMN YADIERTINE 350
    LGEKARKNEL AIEDMDGGTF TISNGGVFGS LFGTPIINPP QSAILGMHGI 400
    FDRPVAVGGK VEVRPMMYVA LTYDHRLIDG REAVTFLRKI KAAVEDPRVL 450
    LLDL 454
    Length:454
    Mass (Da):48,925
    Last modified:April 12, 2005 - v2
    Checksum:i2818F530F4B7C683
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131S → M in BAA14397. (PubMed:1918017)Curated
    Sequence conflicti52 – 543NSS → TVA in BAA14397. (PubMed:1918017)Curated
    Sequence conflicti164 – 1641Y → H in BAA14397. (PubMed:1918017)Curated
    Sequence conflicti281 – 2811F → L in BAA14397. (PubMed:1918017)Curated
    Sequence conflicti448 – 4481R → A in BAA14397. (PubMed:1918017)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC083858 mRNA. Translation: AAH83858.1.
    D90401 mRNA. Translation: BAA14397.1.
    PIRiA41015.
    RefSeqiNP_001006982.2. NM_001006981.2.
    UniGeneiRn.99702.

    Genome annotation databases

    GeneIDi299201.
    KEGGirno:299201.
    UCSCiRGD:1359615. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC083858 mRNA. Translation: AAH83858.1 .
    D90401 mRNA. Translation: BAA14397.1 .
    PIRi A41015.
    RefSeqi NP_001006982.2. NM_001006981.2.
    UniGenei Rn.99702.

    3D structure databases

    ProteinModelPortali Q01205.
    SMRi Q01205. Positions 221-454.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q01205. 1 interaction.

    PTM databases

    PhosphoSitei Q01205.

    Proteomic databases

    PaxDbi Q01205.
    PRIDEi Q01205.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 299201.
    KEGGi rno:299201.
    UCSCi RGD:1359615. rat.

    Organism-specific databases

    CTDi 1743.
    RGDi 1359615. Dlst.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281563.
    HOVERGENi HBG000268.
    InParanoidi Q01205.
    KOi K00658.
    PhylomeDBi Q01205.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .
    BRENDAi 2.3.1.61. 5301.

    Miscellaneous databases

    NextBioi 644993.
    PROi Q01205.

    Gene expression databases

    Genevestigatori Q01205.

    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. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    2. "Purification and molecular cloning of succinyltransferase of the rat alpha-ketoglutarate dehydrogenase complex. Absence of a sequence motif of the putative E3 and/or E1 binding site."
      Nakano K., Matuda S., Yamanaka T., Tsubouchi H., Nakagawa S., Titani K., Ohta S., Miyata T.
      J. Biol. Chem. 266:19013-19017(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-454, PROTEIN SEQUENCE OF 69-83.
      Tissue: Heart.
    3. Lubec G., Chen W.-Q., Afjehi-Sadat L., Diao W.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 69-89; 135-145; 262-308 AND 314-326, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus and Spinal cord.

    Entry informationi

    Entry nameiODO2_RAT
    AccessioniPrimary (citable) accession number: Q01205
    Secondary accession number(s): Q5XI35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 126 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

    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