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P36413

- ODP2_DICDI

UniProt

P36413 - ODP2_DICDI

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

pdhC

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (04 Dec 2007)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

    Catalytic activityi

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

    Cofactori

    Binds 2 lipoyl cofactors covalently.By similarity

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Glycolysis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
    Alternative name(s):
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
    Pyruvate dehydrogenase complex component E2
    Short name:
    PDC-E2
    Short name:
    PDCE2
    Gene namesi
    Name:pdhC
    Synonyms:dlaA
    ORF Names:DDB_G0277847
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 3, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0277847. pdhC.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. pyruvate dehydrogenase complex Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 635Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000020480
    Transit peptidei1 – ?Mitochondrion

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei124 – 1241N6-lipoyllysineBy similarity
    Modified residuei247 – 2471N6-lipoyllysineBy similarity

    Proteomic databases

    PRIDEiP36413.

    Interactioni

    Subunit structurei

    20 to 30 alpha(2)-beta2 tetramers of E1 + 6 homodimers of E3 + 60 copies of E2.

    Protein-protein interaction databases

    STRINGi44689.DDB_0215387.

    Structurei

    3D structure databases

    ProteinModelPortaliP36413.
    SMRiP36413. Positions 79-173, 402-635.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini84 – 15976Lipoyl-binding 1Add
    BLAST
    Domaini207 – 28276Lipoyl-binding 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni340 – 37940E3-binding siteBy similarityAdd
    BLAST
    Regioni403 – 635233CatalyticBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi301 – 31414Ser/Thr-rich (hinge)Add
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 2 lipoyl-binding domains.Curated

    Keywords - Domaini

    Lipoyl, Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    KOiK00627.
    OMAiMEMESYE.
    PhylomeDBiP36413.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR001078. 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. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P36413-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRAINQNSA KVVKSLKQQL VVLEATNVVA YTGTKSFTTT KTFNNTQTKP    50
    KIFTSSNVLS FSSPSSSNVF SEILNKRSYS SKGKEITMPA LSPSMTEGNI 100
    VQWKKKEGDQ IKAGDVIAEV ETDKATMDFQ YEDGNGYLAK ILIPEGTKGI 150
    EINKPIAIIV SKKEDIESAV KNYKPSSQAS STPVQEEAPK PKQEAPKKST 200
    KTYPAHKVVG MPALSPSMET GGIASWTKKE GDQIKAGDAI AEVETDKATM 250
    DFQYEDGNGY LAKILVPGGT SGIQINQPVC IIVKNKEDCD KFADYSVEEQ 300
    SSSSSSSSQE STPSSSSSSS QESTPSQSSS QQTTRKSGER IFATPAARFE 350
    ASSKGYDLSA INGTGPNNRI LKADVLEFVP QKQEVAQQQQ QQTTTTTKKP 400
    TTPTSSGEFT DIPHSNIRKV TAARLTESKQ TIPHYYLTME CRVDKLLKLR 450
    SELNAMNTVK ISVNDFIVKA SAAALRDNPV VNSTWTDQFI RRYHNIDINV 500
    AVNTPQGLFT PIVRGVDMKG LNSISTSVKQ LAEKAQNGKL HPSEFESGTF 550
    TISNLGMLGI KQFAAVINPP QAAILAVGTT ETRVVLSNKP DSPYETATIL 600
    SVTLSCDHRV IDGAVGAEWL KSFKDYVENP IKLIL 635
    Length:635
    Mass (Da):68,986
    Last modified:December 4, 2007 - v2
    Checksum:iDC1B4924A680B2AB
    GO

    Sequence cautioni

    The sequence AAA16511.1 differs from that shown. Reason: Frameshift at positions 577 and 585.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971E → V in AAA16511. 1 PublicationCurated
    Sequence conflicti118 – 1181A → R in AAA16511. 1 PublicationCurated
    Sequence conflicti129 – 1302FQ → S in AAA16511. 1 PublicationCurated
    Sequence conflicti472 – 4732AA → LP in AAA16511. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000023 Genomic DNA. Translation: EAL68096.1.
    U06634 mRNA. Translation: AAA16511.1. Frameshift.
    RefSeqiXP_642438.1. XM_637346.1.

    Genome annotation databases

    EnsemblProtistsiDDB0215387; DDB0215387; DDB_G0277847.
    GeneIDi8621644.
    KEGGiddi:DDB_G0277847.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000023 Genomic DNA. Translation: EAL68096.1 .
    U06634 mRNA. Translation: AAA16511.1 . Frameshift.
    RefSeqi XP_642438.1. XM_637346.1.

    3D structure databases

    ProteinModelPortali P36413.
    SMRi P36413. Positions 79-173, 402-635.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0215387.

    Proteomic databases

    PRIDEi P36413.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0215387 ; DDB0215387 ; DDB_G0277847 .
    GeneIDi 8621644.
    KEGGi ddi:DDB_G0277847.

    Organism-specific databases

    dictyBasei DDB_G0277847. pdhC.

    Phylogenomic databases

    eggNOGi COG0508.
    KOi K00627.
    OMAi MEMESYE.
    PhylomeDBi P36413.

    Miscellaneous databases

    PROi P36413.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi 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. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    2. "Dihydrolipoamide transacetylase gene from Dictyostelium discoideum."
      Mueller-Taubenberger A.
      Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-635.
      Strain: AX2.
    3. Bienvenut W.V., Veltman D.M., Insall R.H.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 141-148; 341-348; 355-369; 461-469 AND 515-529, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiODP2_DICDI
    AccessioniPrimary (citable) accession number: P36413
    Secondary accession number(s): Q54XW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: December 4, 2007
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3