ODP2_NEUCR
ID ODP2_NEUCR Reviewed; 458 AA.
AC P20285; Q7RVH2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial;
DE EC=2.3.1.12;
DE AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE AltName: Full=MRP3;
DE AltName: Full=Pyruvate dehydrogenase complex component E2;
DE Short=PDC-E2;
DE Short=PDCE2;
DE Flags: Precursor;
GN Name=mrp-3; ORFNames=NCU07659;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 29-50.
RX PubMed=2521217; DOI=10.1016/s0021-9258(17)31260-7;
RA Kreader C.A., Langer C.S., Heckman J.E.;
RT "A mitochondrial protein from Neurospora crassa detected both on ribosomes
RT and in membrane fractions. Analysis of the gene, the message, and the
RT protein.";
RL J. Biol. Chem. 264:317-327(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP PROBABLE FUNCTION.
RX PubMed=1825611; DOI=10.1016/0167-4838(91)90271-z;
RA Russel G.C., Guest J.R.;
RT "Sequence similarities within the family of dihydrolipoamide
RT acyltransferases and discovery of a previously unidentified fungal
RT enzyme.";
RL Biochim. Biophys. Acta 1076:225-232(1991).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- MISCELLANEOUS: The E2 component contains covalently-bound lipoyl
CC cofactors and it participates in the generation of acetyl groups from
CC hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme
CC A.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a ribosomal protein.
CC {ECO:0000305|PubMed:2521217}.
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DR EMBL; J04432; AAA60452.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA33550.1; -; Genomic_DNA.
DR PIR; A30775; A30775.
DR RefSeq; XP_962786.1; XM_957693.3.
DR PDB; 6ZLM; EM; 4.30 A; A/AA/AB/B/BA/C/CA/CB/D/DB/E/EA/EB/F/FA/FB/G/GA/GB/H/HA/I/IA/IB/J/JB/KA/KB/L/LA=1-458.
DR PDB; 6ZLO; EM; 2.90 A; A/AA/AB/B/BA/BB/C/CA/CB/D/DA/DB/E/EA/EB/F/FA/FB/G/GA/GB/H/HA/HB/I/IA/IB/J/JA/K=227-458.
DR PDBsum; 6ZLM; -.
DR PDBsum; 6ZLO; -.
DR AlphaFoldDB; P20285; -.
DR SMR; P20285; -.
DR STRING; 5141.EFNCRP00000007764; -.
DR PRIDE; P20285; -.
DR EnsemblFungi; EAA33550; EAA33550; NCU07659.
DR GeneID; 3878934; -.
DR KEGG; ncr:NCU07659; -.
DR VEuPathDB; FungiDB:NCU07659; -.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; P20285; -.
DR OMA; TMEFESF; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR006257; LAT1.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; PTHR23151; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing; Glycolysis;
KW Lipoyl; Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2521217"
FT CHAIN 29..458
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex, mitochondrial"
FT /id="PRO_0000020481"
FT DOMAIN 34..110
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 177..214
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 126..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 431
FT /evidence="ECO:0000255"
FT ACT_SITE 435
FT /evidence="ECO:0000255"
FT MOD_RES 75
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
SQ SEQUENCE 458 AA; 48620 MW; 902A30C76ECA8149 CRC64;
MIVPVLSRQA LRHASVARVA LPSLTRWYAS YPPHTVVKMP ALSPTMTSGG IGAWQKKPGD
KIEPGEVLVE IETDKAQMDF EFQEEGVLAK ILKDSGEKDV AVGNPIAILV EEGTDVNAFK
DFTLKDAGGE TSPAVPKDEP KNESTASAPT PAPTPAPEPE NTSFTGRFQT ALEREPNALP
AAKRLAREKG IDLRNVKGSG PGGKITEEDV KKALASAPAA GAAAAAYTDV PISGMRKTIA
ARLKESVTEN PHFFVSTNLS VSKLLKLRQA LNSSADGRYK LSVNDFLIKA MGIASKRVPT
VNSSWRDGVI RQFETVDVSV AVATPNGLIT PIVKGVEGKG LESISAAVKE LAKKARDGKL
KPEEYQGGSI SISNMGMNPA VQSFTAIINP PQAAILAVGA PQKVAVPVEN EDGTTGVSWD
EQIIVTASFD HKVVDGAVGA EWIRELKKVI ENPLELLL
