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P52993

- ODO2_CUPNH

UniProt

P52993 - ODO2_CUPNH

Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene

sucB

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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 three 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.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei387 – 3871By similarity
    Active sitei391 – 3911By similarity

    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

    BioCyciCNEC381666:GJUJ-2292-MONOMER.
    UniPathwayiUPA00868; UER00840.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (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
    Gene namesi
    Name:sucB
    Synonyms:odhB
    Ordered Locus Names:H16_A2324
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000008210: Chromosome 1

    Subcellular locationi

    GO - Cellular componenti

    1. oxoglutarate dehydrogenase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexPRO_0000162253Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441N6-lipoyllysineSequence Analysis

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.

    Protein-protein interaction databases

    STRINGi381666.H16_A2324.

    Structurei

    3D structure databases

    ProteinModelPortaliP52993.
    SMRiP52993. Positions 185-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7777Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Lipoyl

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281563.
    KOiK00658.
    OMAiVRTYADQ.
    OrthoDBiEOG610413.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    TIGRFAMsiTIGR01347. sucB. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P52993-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIVDVKVPQ LSESVAEATM LNWKKKPGEA VAQDEILIEI ETDKVVLEVP    50
    APSAGVLSII VKNDGDTVVA DEIIAKIDTE ATAGAAAPAA AAPAPAAAAP 100
    APAAAVAAPA AAGGVAMPSA AKLMAEAGLS AGQVAGTGKD GRITKGDALA 150
    AAAAPAAKAA PAPAAAKPAL QQVSAPVDFA ALGDRPEERV PMSRLRARIA 200
    ERLLQSQSTN AILTTFNEVN MKPVMDLRNK YKDRFEKEHG VKLGFMSFFV 250
    KAAVHALKKF PLINASIDGN DIVYHGYFDI GIAVGSPRGL VVPILRNADQ 300
    MSLADIEKKI AEFGVKARDG KLSLEELTGG TFSISNGGVF GSMLSTPIIN 350
    PPQSAILGVH ATKDRPVVED GQIVIRPMNY LAMSYDHRII DGREAVLGLV 400
    AMKDALEDPA RLLLDL 416
    Length:416
    Mass (Da):43,250
    Last modified:October 1, 1996 - v1
    Checksum:i100D839352D0A8DF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91877 Genomic DNA. Translation: CAA62981.1.
    AM260479 Genomic DNA. Translation: CAJ93420.1.
    PIRiT44423.
    RefSeqiYP_726788.1. NC_008313.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ93420; CAJ93420; H16_A2324.
    GeneIDi4249724.
    KEGGireh:H16_A2324.
    PATRICi35234167. VBIRalEut6770_2730.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91877 Genomic DNA. Translation: CAA62981.1 .
    AM260479 Genomic DNA. Translation: CAJ93420.1 .
    PIRi T44423.
    RefSeqi YP_726788.1. NC_008313.1.

    3D structure databases

    ProteinModelPortali P52993.
    SMRi P52993. Positions 185-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 381666.H16_A2324.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ93420 ; CAJ93420 ; H16_A2324 .
    GeneIDi 4249724.
    KEGGi reh:H16_A2324.
    PATRICi 35234167. VBIRalEut6770_2730.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281563.
    KOi K00658.
    OMAi VRTYADQ.
    OrthoDBi EOG610413.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .
    BioCyci CNEC381666:GJUJ-2292-MONOMER.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    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 and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex."
      Hein S., Steinbuechel A.
      FEMS Microbiol. Lett. 136:231-238(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

    Entry informationi

    Entry nameiODO2_CUPNH
    AccessioniPrimary (citable) accession number: P52993
    Secondary accession number(s): Q0K9A1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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