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P36413 (ODP2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:pdhC
Synonyms:dlaA
ORF Names:DDB_G0277847
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length635 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 2 lipoyl cofactors covalently By similarity.

Subunit structure

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

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 2 lipoyl-binding domains.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 635Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000020480

Regions

Domain84 – 15976Lipoyl-binding 1
Domain207 – 28276Lipoyl-binding 2
Region340 – 37940E3-binding site By similarity
Region403 – 635233Catalytic By similarity
Compositional bias301 – 31414Ser/Thr-rich (hinge)

Amino acid modifications

Modified residue1241N6-lipoyllysine By similarity
Modified residue2471N6-lipoyllysine By similarity

Experimental info

Sequence conflict971E → V in AAA16511. Ref.2
Sequence conflict1181A → R in AAA16511. Ref.2
Sequence conflict129 – 1302FQ → S in AAA16511. Ref.2
Sequence conflict472 – 4732AA → LP in AAA16511. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P36413 [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: DC1B4924A680B2AB

FASTA63568,986
        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 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFI02000023 Genomic DNA. Translation: EAL68096.1.
U06634 mRNA. Translation: AAA16511.1. Frameshift.
RefSeqXP_642438.1. XM_637346.1.

3D structure databases

ProteinModelPortalP36413.
SMRP36413. Positions 79-173, 402-635.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0215387.

Proteomic databases

PRIDEP36413.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0215387; DDB0215387; DDB_G0277847.
GeneID8621644.
KEGGddi:DDB_G0277847.

Organism-specific databases

dictyBaseDDB_G0277847. pdhC.

Phylogenomic databases

eggNOGCOG0508.
OMAMEMESYE.
PhylomeDBP36413.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

PROP36413.

Entry information

Entry nameODP2_DICDI
AccessionPrimary (citable) accession number: P36413
Secondary accession number(s): Q54XW4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 4, 2007
Last modified: July 9, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase