ODP2_PSEAE
ID ODP2_PSEAE Reviewed; 547 AA.
AC Q59638;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex;
DE EC=2.3.1.12;
DE AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE AltName: Full=E2;
GN Name=aceF; Synonyms=aceB {ECO:0000303|PubMed:9171401};
GN OrderedLocusNames=PA5016;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAO;
RX PubMed=9171401; DOI=10.1128/jb.179.11.3561-3571.1997;
RA Rae J.L., Cutfield J.F., Lamont I.L.;
RT "Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 179:3561-3571(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 2 lipoyl cofactors covalently. {ECO:0000250};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry.
CC -!- INDUCTION: Induced by glucose. {ECO:0000269|PubMed:9171401}.
CC -!- DISRUPTION PHENOTYPE: Disruption inactivates the pyruvate dehydrogenase
CC complex and causes an increase in pyruvate concentration and acidity of
CC the culture medium. {ECO:0000269|PubMed:9171401}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U47920; AAC45354.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08401.1; -; Genomic_DNA.
DR PIR; H83018; H83018.
DR RefSeq; NP_253703.1; NC_002516.2.
DR RefSeq; WP_003115359.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q59638; -.
DR SMR; Q59638; -.
DR STRING; 287.DR97_2371; -.
DR World-2DPAGE; 0008:Q59638; -.
DR PaxDb; Q59638; -.
DR PRIDE; Q59638; -.
DR EnsemblBacteria; AAG08401; AAG08401; PA5016.
DR GeneID; 881297; -.
DR KEGG; pae:PA5016; -.
DR PATRIC; fig|208964.12.peg.5257; -.
DR PseudoCAP; PA5016; -.
DR HOGENOM; CLU_016733_10_0_6; -.
DR InParanoid; Q59638; -.
DR OMA; TMEFESF; -.
DR PhylomeDB; Q59638; -.
DR BioCyc; PAER208964:G1FZ6-5132-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031405; F:lipoic acid binding; 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; IPR006256; AcTrfase_Pyrv_DH_cplx.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178:SF2; PTHR43178:SF2; 3.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 2.
DR TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Glycolysis; Lipoyl; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..547
FT /note="Dihydrolipoyllysine-residue acetyltransferase
FT component of pyruvate dehydrogenase complex"
FT /id="PRO_0000162283"
FT DOMAIN 2..75
FT /note="Lipoyl-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 119..193
FT /note="Lipoyl-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 248..285
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 75..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 520
FT /evidence="ECO:0000255"
FT MOD_RES 41
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 159
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 225
FT /note="A -> V (in Ref. 1; AAC45354)"
FT /evidence="ECO:0000305"
FT CONFLICT 295..301
FT /note="GGAGATG -> AVPAPR (in Ref. 1; AAC45354)"
FT /evidence="ECO:0000305"
FT CONFLICT 328..329
FT /note="MQ -> IE (in Ref. 1; AAC45354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 56709 MW; 24E15CCC9A590CB4 CRC64;
MSELIRVPDI GNGEGEVIEL LVKPGDKVEA DQSLLTLESD KASMEIPSPK AGVVKSIKAK
VGDTLKEGDE ILELEVEGGE QPAEAKAEAA PAQPEAPKAE APAPAPSESK PAAPAAASVQ
DIKVPDIGSA GKANVIEVMV KAGDTVEADQ SLITLESDKA SMEIPSPASG VVESVSIKVG
DEVGTGDLIL KLKVEGAAPA AEEQPAAAPA QAAAPAAEQK PAAAAPAPAK ADTPAPVGAP
SRDGAKVHAG PAVRMLAREF GVELSEVKAS GPKGRILKED VQVFVKEQLQ RAKSGGAGAT
GGAGIPPIPE VDFSKFGEVE EVAMTRLMQV GAANLHRSWL NVPHVTQFDQ SDITDMEAFR
VAQKAAAEKA GVKLTVLPIL LKACAHLLKE LPDFNSSLAP SGKALIRKKY VHIGFAVDTP
DGLLVPVIRD VDRKSLLQLA AEAADLADKA RNKKLSADAM QGACFTISSL GHIGGTGFTP
IVNAPEVAIL GVSKATMQPV WDGKAFQPRL MLPLSLSYDH RVINGAAAAR FTKRLGELLA
DIRTLLL
