Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P86219

- ODO2_MESAU

UniProt

P86219 - ODO2_MESAU

Protein

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

Gene

DLST

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 16 (01 Oct 2014)
      Sequence version 1 (15 Jun 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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) By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei119 – 1191By similaritySequence Analysis
    Active sitei123 – 1231By similaritySequence 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

    UniPathwayiUPA00868; UER00840.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialBy similarity (EC:2.3.1.61)
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex component E2By similarity
    Short name:
    OGDC-E2By similarity
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complexBy similarity
    E2KBy similarity
    Gene namesi
    Name:DLSTBy similarity
    OrganismiMesocricetus auratus (Golden hamster)
    Taxonomic identifieri10036 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 145›145Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000394748Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei36 – 361N6-acetyllysineBy similarity
    Modified residuei66 – 661N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP86219.

    Interactioni

    Subunit structurei

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 3128Lipoyl-bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Lipoyl

    Family and domain databases

    Gene3Di3.30.559.10. 2 hits.
    InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
    IPR023213. CAT-like_dom.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragments.

    P86219-1 [UniParc]FASTAAdd to Basket

    « Hide

    NDVITVQTPA FAESVTEGDV RVEGGTPLFT LRHNLKLGFM SAFVKASAFA    50
    LQEQPVVNAV IDDATKEVVY RDYIDISVAV ATPRGLVVPV IRNVETMNYA 100
    DIERVEVRPM MYVALTYDHR LIDGREAVTF LRAAVEDPRV LLLDL 145
    Length:145
    Mass (Da):16,122
    Last modified:June 15, 2010 - v1
    Checksum:i32D674B5DD798BBD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-adjacent residuesi21 – 222Curated
    Non-adjacent residuesi32 – 332Curated
    Non-adjacent residuesi104 – 1052Curated
    Non-adjacent residuesi132 – 1332Curated

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P86219.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .

    Family and domain databases

    Gene3Di 3.30.559.10. 2 hits.
    InterProi IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR023213. CAT-like_dom.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
      Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
      Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiODO2_MESAU
    AccessioniPrimary (citable) accession number: P86219
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 16 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3