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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

pdhC

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

(R)-lipoateBy similarityNote: 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
Complete GO annotation...

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
Complete GO annotation...

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 similarityPROSITE-ProRule annotation
Modified residuei247 – 2471N6-lipoyllysineBy similarityPROSITE-ProRule annotation

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
Domaini83 – 16078Lipoyl-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini206 – 28378Lipoyl-binding 2PROSITE-ProRule annotationAdd
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.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Lipoyl, Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
InParanoidiP36413.
KOiK00627.
OMAiYEDGNGY.
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

        10         20         30         40         50
MLRAINQNSA KVVKSLKQQL VVLEATNVVA YTGTKSFTTT KTFNNTQTKP
60 70 80 90 100
KIFTSSNVLS FSSPSSSNVF SEILNKRSYS SKGKEITMPA LSPSMTEGNI
110 120 130 140 150
VQWKKKEGDQ IKAGDVIAEV ETDKATMDFQ YEDGNGYLAK ILIPEGTKGI
160 170 180 190 200
EINKPIAIIV SKKEDIESAV KNYKPSSQAS STPVQEEAPK PKQEAPKKST
210 220 230 240 250
KTYPAHKVVG MPALSPSMET GGIASWTKKE GDQIKAGDAI AEVETDKATM
260 270 280 290 300
DFQYEDGNGY LAKILVPGGT SGIQINQPVC IIVKNKEDCD KFADYSVEEQ
310 320 330 340 350
SSSSSSSSQE STPSSSSSSS QESTPSQSSS QQTTRKSGER IFATPAARFE
360 370 380 390 400
ASSKGYDLSA INGTGPNNRI LKADVLEFVP QKQEVAQQQQ QQTTTTTKKP
410 420 430 440 450
TTPTSSGEFT DIPHSNIRKV TAARLTESKQ TIPHYYLTME CRVDKLLKLR
460 470 480 490 500
SELNAMNTVK ISVNDFIVKA SAAALRDNPV VNSTWTDQFI RRYHNIDINV
510 520 530 540 550
AVNTPQGLFT PIVRGVDMKG LNSISTSVKQ LAEKAQNGKL HPSEFESGTF
560 570 580 590 600
TISNLGMLGI KQFAAVINPP QAAILAVGTT ETRVVLSNKP DSPYETATIL
610 620 630
SVTLSCDHRV IDGAVGAEWL KSFKDYVENP IKLIL
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000023 Genomic DNA. Translation: EAL68096.1.
U06634 mRNA. Translation: AAA16511.1. Frameshift.
RefSeqiXP_642438.1. XM_637346.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi44689.DDB_0215387.

Proteomic databases

PRIDEiP36413.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

dictyBaseiDDB_G0277847. pdhC.

Phylogenomic databases

eggNOGiCOG0508.
InParanoidiP36413.
KOiK00627.
OMAiYEDGNGY.
PhylomeDBiP36413.

Miscellaneous databases

PROiP36413.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 110 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.