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P0AFG7

- ODO2_ECO57

UniProt

P0AFG7 - ODO2_ECO57

Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene

sucB

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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 sitei376 – 3761By similarity
    Active sitei380 – 3801By 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

    BioCyciECOL386585:GJFA-747-MONOMER.
    ECOO157:SUCB-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
    Ordered Locus Names:Z0881, ECs0752
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. oxoglutarate dehydrogenase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 405404Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexPRO_0000162263Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441N6-lipoyllysineBy similarity
    Modified residuei148 – 1481N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP0AFG7.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    MINTiMINT-1242594.
    STRINGi155864.Z0881.

    Structurei

    Secondary structure

    1
    405
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi118 – 1258
    Helixi129 – 1313
    Beta strandi136 – 1394
    Helixi143 – 1497

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CYUNMR-A113-152[»]
    ProteinModelPortaliP0AFG7.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AFG7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7776Lipoyl-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.
    OMAiMMSTPIV.
    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.

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

    P0AFG7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSVDILVPD LPESVADATV ATWHKKPGDA VVRDEVLVEI ETDKVVLEVP    50
    ASADGILDAV LEDEGTTVTS RQILGRLREG NSAGKETSAK SEEKASTPAQ 100
    RQQASLEEQN NDALSPAIRR LLAEHNLDAS AIKGTGVGGR LTREDVEKHL 150
    AKAPAKESAP AAAAPAAQPA LAARSEKRVP MTRLRKRVAE RLLEAKNSTA 200
    MLTTFNEVNM KPIMDLRKQY GEAFEKRHGI RLGFMSFYVK AVVEALKRYP 250
    EVNASIDGDD VVYHNYFDVS MAVSTPRGLV TPVLRDVDTL GMADIEKKIK 300
    ELAVKGRDGK LTVEDLTGGN FTITNGGVFG SLMSTPIINP PQSAILGMHA 350
    IKDRPMAVNG QVEILPMMYL ALSYDHRLID GRESVGFLVT IKELLEDPTR 400
    LLLDV 405
    Length:405
    Mass (Da):44,011
    Last modified:January 23, 2007 - v2
    Checksum:i8439E48C6D381277
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG55051.1.
    BA000007 Genomic DNA. Translation: BAB34175.1.
    PIRiG85573.
    H90722.
    RefSeqiNP_286443.1. NC_002655.2.
    NP_308779.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG55051; AAG55051; Z0881.
    BAB34175; BAB34175; BAB34175.
    GeneIDi917484.
    957834.
    KEGGiece:Z0881.
    ecs:ECs0752.
    PATRICi18350526. VBIEscCol44059_0774.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG55051.1 .
    BA000007 Genomic DNA. Translation: BAB34175.1 .
    PIRi G85573.
    H90722.
    RefSeqi NP_286443.1. NC_002655.2.
    NP_308779.1. NC_002695.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CYU NMR - A 113-152 [» ]
    ProteinModelPortali P0AFG7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1242594.
    STRINGi 155864.Z0881.

    Proteomic databases

    PRIDEi P0AFG7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG55051 ; AAG55051 ; Z0881 .
    BAB34175 ; BAB34175 ; BAB34175 .
    GeneIDi 917484.
    957834.
    KEGGi ece:Z0881.
    ecs:ECs0752.
    PATRICi 18350526. VBIEscCol44059_0774.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .
    BioCyci ECOL386585:GJFA-747-MONOMER.
    ECOO157:SUCB-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AFG7.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiODO2_ECO57
    AccessioniPrimary (citable) accession number: P0AFG7
    Secondary accession number(s): P07016
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 73 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3