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P45303

- ODO1_HAEIN

UniProt

P45303 - ODO1_HAEIN

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

sucA

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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

    2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

    Cofactori

    Thiamine pyrophosphate.By similarity

    GO - Molecular functioni

    1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB-EC
    2. thiamine pyrophosphate binding Source: InterPro

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW
    2. tricarboxylic acid cycle Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Thiamine pyrophosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.2)
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenase
    Gene namesi
    Name:sucA
    Ordered Locus Names:HI_1662
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000000579: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9359352-oxoglutarate dehydrogenase E1 componentPRO_0000162194Add
    BLAST

    Proteomic databases

    PRIDEiP45303.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi71421.HI1662.

    Structurei

    3D structure databases

    ProteinModelPortaliP45303.
    SMRiP45303. Positions 88-934.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0567.
    KOiK00164.
    OMAiGHQNANL.
    OrthoDBiEOG6V1M1F.
    PhylomeDBiP45303.

    Family and domain databases

    Gene3Di3.40.50.970. 2 hits.
    InterProiIPR011603. 2oxoglutarate_DH_E1.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view]
    PANTHERiPTHR23152. PTHR23152. 1 hit.
    PfamiPF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTiSM00861. Transket_pyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 2 hits.
    TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P45303-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQQNKAFDDW LASTALGGAN QSYIEELYES YLSDPQSVEE SWRKTFDSLP    50
    KTTALEQPHT PVRDYFRRLA RENHNEAVTV IDPAAGAKLV KVLQFINAYR 100
    FRGHLEANLD PLNYYRWKVS FVPELDYRHH GFTEQDLNET FNINHYVYKR 150
    DTIKLGELAQ MLKETYCGSI GLEFMHVQDM EQKMWLQSKM ESLLDKPLFT 200
    SEERVNFLRE LTAADGLERY LGAKFPGAKR FSLEGSDAFI PLMKEIIRHS 250
    SRQGVNDVVM GMAHRGRLNM LVNVLGKKPE NLFDEFAGKH SSERTGDVKY 300
    HQGFSSDFAV DDKRVHLTLA FNPSHLEIVS PVVIGSVRSR QTRMNDTEHS 350
    KVLAITVHGD SAVAGQGVVQ ETLNMSNTRG YSVGGTIRIV INNQIGFTTS 400
    NPNDTRSTEY CTDIAKMIQA PIIHVNGDDP EAVAFAARMA VEYRNLFKRD 450
    IFIDLISYRR HGHNEADEPL ATQPMMYSII KKHPTPRKVY ADRLVSEGVM 500
    TEEQVTEMAN DYRDALDNGD RVVSEWREMD TAKMDWLQYL NYDWTAPYES 550
    KFSQERFLTL AKRVCEYPES LRAHPRVEKI YNDRKAMYQG EKLLDWGMAE 600
    TMAYATLLDE GVNVRLSGED AGRGTFFHRH AVVHNQNDGT GYVPLTHLHA 650
    NQGRFEVWDS VLSEESVLAF EYGYATTDPK TLTIWEAQFG DFANGAQIVI 700
    DQFISSGEQK WGRMCGLVML LPHGYEGQGP EHSSARLERY LQLCAEQNMQ 750
    VCVPSTPAQV YHMLRRQSLR KMRRPLIAIS PKSLLRHPLA VSSLDELING 800
    TFQTVIGEID ELDPKDVKRV VMCSGKVYYD LLEQRRANNQ KDVAIIRIEQ 850
    LYPFPHEDVK KALEPYAHVT DYVWCQEEPL NQGAWYCSKH NFESAIPESV 900
    KLKYAGRPAS ASPAVGYMSL HTKQQKQLVE DALSF 935
    Length:935
    Mass (Da):106,806
    Last modified:November 1, 1995 - v1
    Checksum:i33607F3C3AFDDC78
    GO

    Sequence cautioni

    The sequence AAC23308.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC23308.1. Different initiation.
    PIRiE64135.
    RefSeqiNP_439804.2. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC23308; AAC23308; HI_1662.
    GeneIDi950496.
    KEGGihin:HI1662.
    PATRICi20192073. VBIHaeInf48452_1740.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC23308.1 . Different initiation.
    PIRi E64135.
    RefSeqi NP_439804.2. NC_000907.1.

    3D structure databases

    ProteinModelPortali P45303.
    SMRi P45303. Positions 88-934.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 71421.HI1662.

    Proteomic databases

    PRIDEi P45303.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC23308 ; AAC23308 ; HI_1662 .
    GeneIDi 950496.
    KEGGi hin:HI1662.
    PATRICi 20192073. VBIHaeInf48452_1740.

    Phylogenomic databases

    eggNOGi COG0567.
    KOi K00164.
    OMAi GHQNANL.
    OrthoDBi EOG6V1M1F.
    PhylomeDBi P45303.

    Family and domain databases

    Gene3Di 3.40.50.970. 2 hits.
    InterProi IPR011603. 2oxoglutarate_DH_E1.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view ]
    PANTHERi PTHR23152. PTHR23152. 1 hit.
    Pfami PF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 2 hits.
    TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

    Entry informationi

    Entry nameiODO1_HAEIN
    AccessioniPrimary (citable) accession number: P45303
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 94 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. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3