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B9EC10

- B9EC10_MACCJ

UniProt

B9EC10 - B9EC10_MACCJ

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Macrococcus caseolyticus (strain JCSC5402)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (24 Mar 2009)
      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).UniRule annotationSAAS annotation

    Catalytic activityi

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

    Cofactori

    Thiamine pyrophosphate.UniRule annotationSAAS annotation

    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

    OxidoreductaseUniRule annotationSAAS annotation

    Keywords - Biological processi

    GlycolysisUniRule annotationSAAS annotation

    Keywords - Ligandi

    Thiamine pyrophosphateUniRule annotationSAAS annotation

    Enzyme and pathway databases

    BioCyciMCAS458233:GI03-1075-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-oxoglutarate dehydrogenase E1 componentUniRule annotation (EC:1.2.4.2UniRule annotation)
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenaseUniRule annotation
    Gene namesi
    Name:odhAUniRule annotation
    Ordered Locus Names:MCCL_1064Imported
    OrganismiMacrococcus caseolyticus (strain JCSC5402)Imported
    Taxonomic identifieri458233 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesMacrococcus
    ProteomesiUP000001383: Chromosome

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotationSAAS annotation

    Protein-protein interaction databases

    STRINGi458233.MCCL_1064.

    Structurei

    3D structure databases

    ProteinModelPortaliB9EC10.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0567.
    HOGENOMiHOG000259588.
    KOiK00164.
    OMAiQHAPNKE.
    OrthoDBiEOG6V1M1F.

    Family and domain databases

    Gene3Di3.40.50.970. 2 hits.
    HAMAPiMF_01169. SucA_OdhA.
    InterProiIPR011603. 2oxoglutarate_DH_E1.
    IPR023784. 2oxoglutarate_DH_E1_bac.
    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.

    B9EC10-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKGKNLEEA PPRFGTNLGI LLEMFDQYQN DPSSVSDELQ ELFSNIQRGS    50
    TGHSGMGSTD ADIVKRLMRL IDNIRQYGHL KADIYPLYKP KRDQHIKLSI 100
    EDFGLSEEVL KQLPASLVSE HYGERLNNAF EAITEMQQTY QGPIAYEVSH 150
    INNSEEREWL KTTIESKVKR DFSKEEKVEL LKSVARVEGF EKYIHKNFVG 200
    AKRFSIEGVD ALVPMLENVI KFAGENNIQD IEIGMAHRGR LNVLTHILEK 250
    PYEMMLSEFM HTDPMKFLPE DGSLVVKKGW TGDVKYHLGG IKTTTRFGKT 300
    QTISLANNPS HLEIVAPVVL GKTRAVQEVT DGVNEPKQDF NKALAVLIHG 350
    DAAFPGQGIN FESMNLSNLK GYSVGGSLHI ITNNRVGFTT ESYDSRSTTY 400
    ATDVAKGYDL PIIHVNADDL EACIEAIEVA MAYRQKFNKD FVIDLVGYRR 450
    YGHNEMDEPT VTNPMLYKEV KGHPSIEILY GKSLVEASVI TEDEMNAIFE 500
    DVASRLRSAH DAIDKSSVNN DSEMKMPEAV EAGYEKIDTG VALEKLKQLN 550
    DDMLSIPEQF SVFNKLQKIL ERRNDPFTKD GLVDWGHAEL LAYGTIIQDG 600
    NPVRHTGQDA ERGTFAHRHA VLHDVKNGDK YIPLQHIEGA QSSFDIHNSP 650
    LSEAAVVGFE YGYNLQNNKA LTVWEAQYGD FANMAQMIFD NFISSAEAKW 700
    GEKSGLTLLL PHAYEGQGPE HSSARLERFL QLAAEHNWTV ANLSSTANYF 750
    HLLRRQAQYL GTDRMRPLVI MSPKSLLRNS FVSDTIEKFT EGSFKAIISS 800
    EYKKTKVKKL LIASGKVAVD LMTELTKNPN DEVHVIRLEQ IYPFPEQDIK 850
    AIIDDLKGLT EIGFVQEEPK NQGSWHYIYP LLNNIKPAKV KLSYYGRPYR 900
    AAPAEGDNEI HKIVQSKLIS EALNI 925
    Length:925
    Mass (Da):104,156
    Last modified:March 24, 2009 - v1
    Checksum:iCF4BA9E54754A667
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP009484 Genomic DNA. Translation: BAH17771.1.
    RefSeqiYP_002560467.1. NC_011999.1.

    Genome annotation databases

    EnsemblBacteriaiBAH17771; BAH17771; MCCL_1064.
    GeneIDi7390741.
    KEGGimcl:MCCL_1064.
    PATRICi22424493. VBIMacCas48391_1189.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP009484 Genomic DNA. Translation: BAH17771.1 .
    RefSeqi YP_002560467.1. NC_011999.1.

    3D structure databases

    ProteinModelPortali B9EC10.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 458233.MCCL_1064.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAH17771 ; BAH17771 ; MCCL_1064 .
    GeneIDi 7390741.
    KEGGi mcl:MCCL_1064.
    PATRICi 22424493. VBIMacCas48391_1189.

    Phylogenomic databases

    eggNOGi COG0567.
    HOGENOMi HOG000259588.
    KOi K00164.
    OMAi QHAPNKE.
    OrthoDBi EOG6V1M1F.

    Enzyme and pathway databases

    BioCyci MCAS458233:GI03-1075-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.970. 2 hits.
    HAMAPi MF_01169. SucA_OdhA.
    InterProi IPR011603. 2oxoglutarate_DH_E1.
    IPR023784. 2oxoglutarate_DH_E1_bac.
    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. "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402, reflecting the ancestral genome of the human-pathogenic staphylococci."
      Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.
      J. Bacteriol. 191:1180-1190(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JCSC5402Imported.

    Entry informationi

    Entry nameiB9EC10_MACCJ
    AccessioniPrimary (citable) accession number: B9EC10
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 24, 2009
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 39 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3