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UniProtKB/Swiss-Prot entry P36413


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODP2_DICDI
Primary accession number P36413
Secondary accession number Q54XW4
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on December 4, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 67)
Name and origin of the protein
Protein name Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial [Precursor]
Synonyms EC 2.3.1.12
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
PDC-E2
E2
Gene name
Name: pdhC
Synonyms: dlaA
ORFNames: DDB_G0277847
From
Dictyostelium discoideum (Slime mold) [TaxID: 44689] 
Taxonomy Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 43-635.
STRAIN=AX2;
Mueller-Taubenberger A.;
"Dihydrolipoamide transacetylase gene from Dictyostelium discoideum.";
Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AAFI02000023; EAL68096.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U06634; AAA16511.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_642438.1; -.
3D structure databases
HSSP P10515; 1FYC. [HSSP ENTRY / PDB]
ModBase P36413.
Organism-specific databases
dictyBase DDB_G0277847; pdhC.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0045254; Cellular component: pyruvate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0004742; Molecular function: dihydrolipoyllysine-residue acetyltransferase activity (inferred from electronic annotation from InterPro).
GO:0031405; Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0006090; Biological process: pyruvate metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003016; 2-oxoA_DHase_lipoyl-BS.
IPR001078; 2Oxoacid_DHase.
IPR006257; AcTrfase_Pyrv_DHase_cplx_L.
IPR000089; Biotin_lipoyl.
IPR004167; E3_bd.
Graphical view of domain structure.
Gene3D G3DSA:4.10.320.10; E3_bd; 2.
Pfam PF00198; 2-oxoacid_dh; 2.
PF00364; Biotin_lipoyl; 4.
PF02817; E3_binding; 2.
Pfam graphical view of domain structure.
ProDom PD001115; 2Oxoacid_dh; 2.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01349; PDHac_trf_mito; 1.
PROSITE PS50968; BIOTINYL_LIPOYL; 2.
PS00189; LIPOYL; 2.
PROSITE graphical view of domain structure (profiles).
ProtoNet P36413.
Genome annotation databases
GeneID 3393169; -.
KEGG ddi:DDB_0215387; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Complete proteome; Glycolysis; Lipoyl; Mitochondrion; Repeat; Transferase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion. 
CHAIN   ?   635        Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial. PRO_0000020480
DOMAIN   84   159  76     Lipoyl-binding 1. 
DOMAIN   207   282  76     Lipoyl-binding 2. 
REGION   340   379  40     E3-binding site (By similarity). 
REGION   403   635  233     Catalytic (By similarity). 
COMPBIAS   301   314  14     Ser/Thr-rich (hinge). 
BINDING   124   124        Lipoyl (covalent) (By similarity). 
BINDING   247   247        Lipoyl (covalent) (By similarity). 
CONFLICT   97    97        E -> V (in Ref. 2; AAA16511). 
CONFLICT   118   118        A -> R (in Ref. 2; AAA16511). 
CONFLICT   129   130        FQ -> S (in Ref. 2; AAA16511). 
CONFLICT   472   473        AA -> LP (in Ref. 2; AAA16511). 
Sequence information
Length: 635 AA [This is the length of the unprocessed precursor] Molecular weight: 68986 Da [This is the MW of the unprocessed precursor] CRC64: DC1B4924A680B2AB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLRAINQNSA KVVKSLKQQL VVLEATNVVA YTGTKSFTTT KTFNNTQTKP KIFTSSNVLS 

        70         80         90        100        110        120 
FSSPSSSNVF SEILNKRSYS SKGKEITMPA LSPSMTEGNI VQWKKKEGDQ IKAGDVIAEV 

       130        140        150        160        170        180 
ETDKATMDFQ YEDGNGYLAK ILIPEGTKGI EINKPIAIIV SKKEDIESAV KNYKPSSQAS 

       190        200        210        220        230        240 
STPVQEEAPK PKQEAPKKST KTYPAHKVVG MPALSPSMET GGIASWTKKE GDQIKAGDAI 

       250        260        270        280        290        300 
AEVETDKATM DFQYEDGNGY LAKILVPGGT SGIQINQPVC IIVKNKEDCD KFADYSVEEQ 

       310        320        330        340        350        360 
SSSSSSSSQE STPSSSSSSS QESTPSQSSS QQTTRKSGER IFATPAARFE ASSKGYDLSA 

       370        380        390        400        410        420 
INGTGPNNRI LKADVLEFVP QKQEVAQQQQ QQTTTTTKKP TTPTSSGEFT DIPHSNIRKV 

       430        440        450        460        470        480 
TAARLTESKQ TIPHYYLTME CRVDKLLKLR SELNAMNTVK ISVNDFIVKA SAAALRDNPV 

       490        500        510        520        530        540 
VNSTWTDQFI RRYHNIDINV AVNTPQGLFT PIVRGVDMKG LNSISTSVKQ LAEKAQNGKL 

       550        560        570        580        590        600 
HPSEFESGTF TISNLGMLGI KQFAAVINPP QAAILAVGTT ETRVVLSNKP DSPYETATIL 

       610        620        630 
SVTLSCDHRV IDGAVGAEWL KSFKDYVENP IKLIL 

P36413 in FASTA format

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View entry in raw text format (no links)
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