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D8RIN1

- D8RIN1_SELML

UniProt

D8RIN1 - D8RIN1_SELML

Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

SELMODRAFT_121442

Organism
Selaginella moellendorffii (Spikemoss)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 20 (01 Oct 2014)
      Sequence version 1 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.UniRule annotation

    Catalytic activityi

    Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.UniRule annotation
    Binds 2 lipoyl cofactors covalently.UniRule annotation
    Binds 3 lipoyl cofactors covalently.UniRule annotation

    GO - Molecular functioni

    1. copper ion binding Source: EnsemblPlants/Gramene
    2. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. pyruvate metabolic process Source: InterPro

    Keywords - Molecular functioni

    AcyltransferaseUniRule annotation, Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
    Gene namesi
    ORF Names:SELMODRAFT_121442Imported, SELMODRAFT_94277Imported
    OrganismiSelaginella moellendorffii (Spikemoss)Imported
    Taxonomic identifieri88036 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaLycopodiidaeSelaginellalesSelaginellaceaeSelaginella
    ProteomesiUP000001514: Unassembled WGS sequence

    Subcellular locationi

    Mitochondrion matrix UniRule annotation

    GO - Cellular componenti

    1. chloroplast envelope Source: EnsemblPlants/Gramene
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. pyruvate dehydrogenase complex Source: InterPro

    Family & Domainsi

    Sequence similaritiesi

    Contains 1 lipoyl-binding domain.UniRule annotation

    Keywords - Domaini

    LipoylUniRule annotation

    Phylogenomic databases

    KOiK00627.

    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.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [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.
    TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    D8RIN1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLFLSILCL TDHVFFSCLV PSHQPLGMPS LSPTMTQGNI VKWKKKEGDK    50
    VTAGDVLCEI ETDKATVDME CMEDGYLAKI VFSDGAKDIK VGQIIAITVE 100
    EQGDIDKFKD YKADAPAAPP KPAPKESPPP PKPTESPKPA PSPKPAPAAS 150
    GDRIIASPNA RKYAQDNQIS LSGVAGTGPG GRIVRADLLI VVFIGGQQVQ 200
    EPRRAETPGD STSLDYTDLP NTQIRRVIAQ RLLQSKQTIP HYYLTVDVRV 250
    DKLLALRTQL NAKLEKEKRK KLSVNDFVLK AAALALKKVP ECNSSWTDEF 300
    IRQFHNINIS VAVQTERGLM VPVVKDADKK GLGAISDDVR TLAEKARENT 350
    LKPSDYDGGT FTVSNLGGPF GIKQFCAIIN PPQSCILAVG TTDKRVIPGE 400
    NDGEYTAATF MSATLSCDHR VVDGAIGAHW LGAFKGYIED PMTLLL 446
    Length:446
    Mass (Da):48,348
    Last modified:October 5, 2010 - v1
    Checksum:iC3C1AEEA63F986D4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GL377630 Genomic DNA. Translation: EFJ13978.1.
    GL377580 Genomic DNA. Translation: EFJ28117.1.
    RefSeqiXP_002970791.1. XM_002970745.1.
    XP_002985103.1. XM_002985057.1.
    UniGeneiSmo.15286.
    Smo.2571.

    Genome annotation databases

    EnsemblPlantsiEFJ13978; EFJ13978; SELMODRAFT_121442.
    EFJ28117; EFJ28117; SELMODRAFT_94277.
    GeneIDi9641347.
    9648948.
    KEGGismo:SELMODRAFT_121442.
    smo:SELMODRAFT_94277.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GL377630 Genomic DNA. Translation: EFJ13978.1 .
    GL377580 Genomic DNA. Translation: EFJ28117.1 .
    RefSeqi XP_002970791.1. XM_002970745.1.
    XP_002985103.1. XM_002985057.1.
    UniGenei Smo.15286.
    Smo.2571.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi EFJ13978 ; EFJ13978 ; SELMODRAFT_121442 .
    EFJ28117 ; EFJ28117 ; SELMODRAFT_94277 .
    GeneIDi 9641347.
    9648948.
    KEGGi smo:SELMODRAFT_121442.
    smo:SELMODRAFT_94277.

    Phylogenomic databases

    KOi K00627.

    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.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [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 TIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Selaginella genome identifies genetic changes associated with the evolution of vascular plants."
      Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D., Chapple C., Cheng C.
      , Correa L.G., Dacre M., DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.
      Science 332:960-963(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiD8RIN1_SELML
    AccessioniPrimary (citable) accession number: D8RIN1
    Entry historyi
    Integrated into UniProtKB/TrEMBL: October 5, 2010
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 20 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