P36413 (ODP2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	pdhC
Synonyms:	dlaA
ORF Names:	DDB_G0277847

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	635 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Lipoyl Repeat Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW pyruvate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell pyruvate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion
	Chain	? – 635		Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial		PRO_0000020480
Regions
	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
	Compositional bias	301 – 314	14	Ser/Thr-rich (hinge)
Amino acid modifications
	Modified residue	124	1	N6-lipoyllysine By similarity
	Modified residue	247	1	N6-lipoyllysine By similarity
Experimental info
	Sequence conflict	97	1	E → V in AAA16511. Ref.2
	Sequence conflict	118	1	A → R in AAA16511. Ref.2
	Sequence conflict	129 – 130	2	FQ → S in AAA16511. Ref.2
	Sequence conflict	472 – 473	2	AA → LP in AAA16511. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P36413 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: DC1B4924A680B2AB	FASTA	635	68,986
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 15875012] [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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000023 Genomic DNA. Translation: EAL68096.1. U06634 mRNA. Translation: AAA16511.1. Frameshift.
RefSeq	XP_642438.1. XM_637346.1.
3D structure databases
ProteinModelPortal	P36413.
SMR	P36413. Positions 79-173, 402-635.
ModBase	Search...
Protein-protein interaction databases
STRING	P36413.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0215387; DDB0215387; DDB_G0277847.
GeneID	8621644.
GenomeReviews	Gene locus pdhC in contig CM000152_GR.
KEGG	ddi:DDB_G0277847.
Organism-specific databases
dictyBase	DDB_G0277847. pdhC.
Phylogenomic databases
eggNOG	KOG0557.
GeneTree	EPrGT00050000004445.
HOGENOM	HBG630916.
OMA	YASPMAK.
PhylomeDB	P36413.
ProtClustDB	CLSZ2442470.
Family and domain databases
InterPro	IPR001078. 2-oxoacid_DH_actylTfrase. IPR006257. AcTrfase_Pyrv_DH_cplx_L. IPR000089. Biotin_lipoyl. IPR023213. CAT-like_dom. IPR004167. E3-bd. IPR011053. Single_hybrid_motif. [Graphical view]
Gene3D	G3DSA:3.30.559.10. CAT-like_dom. 1 hit. G3DSA:4.10.320.10. E3_bd. 1 hit.
KO	K00627.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 2 hits. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 2 hits.
TIGRFAMs	TIGR01349. PDHac_trf_mito. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 2 hits. PS00189. LIPOYL. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_DICDI

Accession

Primary (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:	November 16, 2011
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)