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Q5HPC7

- ODO2_STAEQ

UniProt

Q5HPC7 - ODO2_STAEQ

Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene

odhB

Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (15 Feb 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 three 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.

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei391 – 3911By similarity
    Active sitei395 – 3951By 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

    BioCyciSEPI176279:GJJB-1011-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:odhB
    Synonyms:sucB
    Ordered Locus Names:SERP0985
    OrganismiStaphylococcus epidermidis (strain ATCC 35984 / RP62A)
    Taxonomic identifieri176279 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000531: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. oxoglutarate dehydrogenase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 420420Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexPRO_0000288108Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421N6-lipoyllysineSequence Analysis

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi176279.SERP0985.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5HPC7.
    SMRiQ5HPC7. Positions 191-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7574Lipoyl-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.
    OMAiQEDETVE.
    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.

    Q5HPC7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEVKVPELA ESITEGTIAE WLKNVGDNVD KGEAILELET DKVNVEVVSE    50
    EAGVLSEQLA EEGDTVEVGQ AVAVVGEGQV NTSNDSSNES SQKDEAKEKE 100
    TPKQSNPNSS ESENTQDNSQ QRINATPSAR RHARKNGVDL SEVSGKGNDV 150
    LRKDDVENSQ KSSSQTAKSE SKSQNSGSKQ TNNNPSKPVI REKMSRRKKT 200
    AAKKLLEVSN QTAMLTTFNE VDMTNVMDLR KRKKEQFIKD HDGTKLGFMS 250
    FFTKAAVAAL KKYPEVNAEI DGDDMITKQF YDIGIAVSTD DGLLVPFVRD 300
    CDKKNFAEIE QEIANLAVKA RDKKLGLDDM VNGSFTITNG GIFGSMMSTP 350
    IINGNQAAIL GMHSIITRPI AVDKDTIENR PMMYIALSYD HRIIDGKEAV 400
    GFLKTIKELI ENPEDLLLES 420
    Length:420
    Mass (Da):46,080
    Last modified:February 15, 2005 - v1
    Checksum:i9A4A04B2923A2F65
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000029 Genomic DNA. Translation: AAW54332.1.
    RefSeqiYP_188563.1. NC_002976.3.

    Genome annotation databases

    EnsemblBacteriaiAAW54332; AAW54332; SERP0985.
    GeneIDi3242078.
    KEGGiser:SERP0985.
    PATRICi19612839. VBIStaEpi130894_0962.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000029 Genomic DNA. Translation: AAW54332.1 .
    RefSeqi YP_188563.1. NC_002976.3.

    3D structure databases

    ProteinModelPortali Q5HPC7.
    SMRi Q5HPC7. Positions 191-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 176279.SERP0985.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW54332 ; AAW54332 ; SERP0985 .
    GeneIDi 3242078.
    KEGGi ser:SERP0985.
    PATRICi 19612839. VBIStaEpi130894_0962.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .
    BioCyci SEPI176279:GJJB-1011-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. "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
      Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H.
      , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
      J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35984 / RP62A.

    Entry informationi

    Entry nameiODO2_STAEQ
    AccessioniPrimary (citable) accession number: Q5HPC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 74 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