Reviewed, UniProtKB/Swiss-Prot P20285 (ODP2_NEUCR)

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
    PDC-E2
      Short name=E2
    MRP3

Gene names

Name:	mrp-3
ORF Names:	NCU07659

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

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
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 lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro
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)
	P20285-1 [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: 2521217] [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: 12712197] [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: 1825611] [Abstract] Cited for: PROBABLE FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J04432 Genomic DNA. Translation: AAA60452.1. AABX02000043 Genomic DNA. Translation: EAA33550.1.
PIR	A30775.
RefSeq	XP_962786.1.
3D structure databases
HSSP	HSSP built from PDB template 1FYC based on UniProtKB P10515.
ModBase	Search...
Protein-protein interaction databases
STRING	P20285.
Genome annotation databases
GeneID	3878934.
KEGG	ncr:NCU07659.
NMPDR	fig|5141.1.peg.6298.
UCSC	E03G2.2. c. elegans.
Enzyme and pathway databases
BioCyc	NCRA-XX3-01:NCRA-XX3-01-002518-MON.
BRENDA	2.3.1.12. 266.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR006257. AcTrfase_Pyrv_DH_cplx_L. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
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:	September 1, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)