P20285 (ODP2_NEUCR) 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
MRP3
Pyruvate dehydrogenase complex component E2
Short name=PDC-E2
Short name=PDCE2

Gene names

Name:	mrp-3
ORF Names:	NCU07659

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora › Neurospora crassa

Protein attributes

Sequence length	458 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). Ref.3
Catalytic activity	Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
Subcellular location	Mitochondrion matrix.
Miscellaneous	The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.
Caution	Was originally (Ref.1) thought to be a ribosomal protein.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Lipoyl Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from electronic annotation. Source: EnsemblFungi glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial pyruvate dehydrogenase complex Inferred from electronic annotation. Source: EnsemblFungi
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 – 28	28	Mitochondrion Ref.1
	Chain	29 – 458	430	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial		PRO_0000020481
Regions
	Domain	35 – 109	75	Lipoyl-binding
Sites
	Active site	431	1	Potential
	Active site	435	1	Potential
Amino acid modifications
	Modified residue	75	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P20285 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 902A30C76ECA8149	FASTA	458	48,620
	10 20 30 40 50 60 MIVPVLSRQA LRHASVARVA LPSLTRWYAS YPPHTVVKMP ALSPTMTSGG IGAWQKKPGD 70 80 90 100 110 120 KIEPGEVLVE IETDKAQMDF EFQEEGVLAK ILKDSGEKDV AVGNPIAILV EEGTDVNAFK 130 140 150 160 170 180 DFTLKDAGGE TSPAVPKDEP KNESTASAPT PAPTPAPEPE NTSFTGRFQT ALEREPNALP 190 200 210 220 230 240 AAKRLAREKG IDLRNVKGSG PGGKITEEDV KKALASAPAA GAAAAAYTDV PISGMRKTIA 250 260 270 280 290 300 ARLKESVTEN PHFFVSTNLS VSKLLKLRQA LNSSADGRYK LSVNDFLIKA MGIASKRVPT 310 320 330 340 350 360 VNSSWRDGVI RQFETVDVSV AVATPNGLIT PIVKGVEGKG LESISAAVKE LAKKARDGKL 370 380 390 400 410 420 KPEEYQGGSI SISNMGMNPA VQSFTAIINP PQAAILAVGA PQKVAVPVEN EDGTTGVSWD 430 440 450 EQIIVTASFD HKVVDGAVGA EWIRELKKVI ENPLELLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A mitochondrial protein from Neurospora crassa detected both on ribosomes and in membrane fractions. Analysis of the gene, the message, and the protein." Kreader C.A., Langer C.S., Heckman J.E. J. Biol. Chem. 264:317-327(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-50.
[2]	"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]	"Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme." Russel G.C., Guest J.R. Biochim. Biophys. Acta 1076:225-232(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROBABLE FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04432 Genomic DNA. Translation: AAA60452.1. AABX02000043 Genomic DNA. Translation: EAA33550.1.
PIR	A30775.
RefSeq	XP_962786.1. XM_957693.2.
UniGene	Ncr.16601.
3D structure databases
ProteinModelPortal	P20285.
SMR	P20285. Positions 28-122, 174-212.
ModBase	Search...
Protein-protein interaction databases
STRING	5141.NCU07659.1.
Proteomic databases
PRIDE	P20285.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFNCRT00000007775; EFNCRP00000007764; EFNCRG00000007763.
GeneID	3878934.
KEGG	ncr:NCU07659.
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281566.
KO	K00627.
OMA	GTICISN.
OrthoDB	EOG4CC78S.
Family and domain databases
Gene3D	3.30.559.10. 1 hit. 4.10.320.10. 1 hit.
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR023213. CAT-like_dom. IPR004167. E3-bd. IPR006257. LAT1. IPR027189. LAT1_fungal. IPR011053. Single_hybrid_motif. [Graphical view]
PANTHER	PTHR23151:SF24. PTHR23151:SF24. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 1 hit.
TIGRFAMs	TIGR01349. PDHac_trf_mito. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_NEUCR

Accession

Primary (citable) accession number: P20285
Secondary accession number(s): Q7RVH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program