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)

P20707

- ODO1_AZOVI

UniProt

P20707 - ODO1_AZOVI

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

sucA

Organism
Azotobacter vinelandii
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      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 three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

    Catalytic activityi

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

    Cofactori

    Thiamine pyrophosphate.

    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

    Enzyme and pathway databases

    SABIO-RKP20707.

    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
    Synonyms:odhA
    OrganismiAzotobacter vinelandii
    Taxonomic identifieri354 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9439432-oxoglutarate dehydrogenase E1 componentPRO_0000162186Add
    BLAST

    Proteomic databases

    PRIDEiP20707.

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    3D structure databases

    ProteinModelPortaliP20707.
    SMRiP20707. Positions 90-943.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    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.

    P20707-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQDSVMQRMW NSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFEKLPA    50
    EAGTSTDVPH APVRDQFVLL AKNQRRAQPV ATSSVSTEHE KKQVEVLRLI 100
    QAYRTRGHQA SQLDPLGLWQ RTAPSDLSIT HYGLTNADLD TPFRTGELYI 150
    GKEEATLREI LQALQETYCR TIGAEFTHIV DSEQRNWFAQ RLESVRGRPV 200
    YSKEAKSHLL ERLSAAEGLE KYLGTKYPGT KRFGLEGGES LVPVVDEIIQ 250
    RSGSYGTKEV VIGMAHRGRL NLLVNALGKN PRDLFDEFEG KHLVELGSGD 300
    VKYHQGFSSN VMTSGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRVDA 350
    TGEKVVPISI HGDSAFAGQG VVMETFQMSQ IRGYKTGGTI HIVVNNQVGF 400
    TTSNPVDTRS TEYCTDPAKM IQAPVLHVNG DDPEAVLFVT QLAVDYRMQF 450
    KRDVVIDLVC YRRRGHNEAD EPSGTQPLMY QKIAKQPTTR ELYADALVKE 500
    GSLSQEEVQA KVDEYRTALD NGQHVLKSLV KEPNTELFVD WTPYLGHAWT 550
    ARHDTSFELK TLQELNAKLL QIPEGFVVQR QVAKILEDRG RMGVGAMPIN 600
    WGCAETLAYA TLLKEGHPVR ITGQDVGRGT FSHRHAALHN QKDASRYIPL 650
    QNLYEGQPKF ELYDSFLSEE AVLAFEYGYA TTTPNALVIW EASSGDFANG 700
    AQVVIDQFIS SGETKWGALC GLTMLLPHGY EGQGPEHSSA RLERYLQLCA 750
    EQNIQVCVPT TPAQVYHMLR RQVIRPLRKP LVALTPKSLL RHKSAISTLE 800
    DLALGSFHPV LPEVDSLDPK KVERLVLCSG KVYYDLLDKR HAEGREDIAI 850
    VRIEQLYPFP EEELAEVMAP YTNLKHVVWC QEEPMNQGAW YCSQHHMRRV 900
    ASAHKKELFL QYAGREASAA PACGYASMHA EQQEKLLQDA FTV 943
    Length:943
    Mass (Da):105,688
    Last modified:February 1, 1991 - v1
    Checksum:iD3F35356D454E2A1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52433 Genomic DNA. Translation: CAA36680.1.
    X52432 Genomic DNA. Translation: CAA36677.1.
    PIRiS07776.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52433 Genomic DNA. Translation: CAA36680.1 .
    X52432 Genomic DNA. Translation: CAA36677.1 .
    PIRi S07776.

    3D structure databases

    ProteinModelPortali P20707.
    SMRi P20707. Positions 90-943.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P20707.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P20707.

    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. "The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component."
      Schulze E., Westphal A.H., Hanemaaijer R., de Kok A.
      Eur. J. Biochem. 187:229-234(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component."
      Westphal A.H., de Kok A.
      Eur. J. Biochem. 187:235-239(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 909-943.

    Entry informationi

    Entry nameiODO1_AZOVI
    AccessioniPrimary (citable) accession number: P20707
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3