ID B7UIG3_ECO27 Unreviewed; 630 AA.
AC B7UIG3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN Name=aceF {ECO:0000313|EMBL:CAS07666.1};
GN OrderedLocusNames=E2348C_0118 {ECO:0000313|EMBL:CAS07666.1};
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07666.1, ECO:0000313|Proteomes:UP000008205};
RN [1] {ECO:0000313|EMBL:CAS07666.1, ECO:0000313|Proteomes:UP000008205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX PubMed=18952797; DOI=10.1128/JB.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
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). {ECO:0000256|ARBA:ARBA00025211}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
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 Evidence={ECO:0000256|ARBA:ARBA00000925,
CC ECO:0000256|RuleBase:RU361137};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU361137};
CC Note=Binds 3 lipoyl cofactors covalently.
CC {ECO:0000256|RuleBase:RU361137};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484,
CC ECO:0000256|RuleBase:RU361137}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM180568; CAS07666.1; -; Genomic_DNA.
DR RefSeq; WP_000963544.1; NC_011601.1.
DR AlphaFoldDB; B7UIG3; -.
DR KEGG; ecg:E2348C_0118; -.
DR HOGENOM; CLU_016733_10_0_6; -.
DR OMA; HPCIMAP; -.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 3.
DR Gene3D; 2.40.50.100; -; 3.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 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 NCBIfam; TIGR01348; PDHac_trf_long; 1.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 3.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 3.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:CAS07666.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008205};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU361137}.
FT DOMAIN 2..75
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 105..178
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 206..279
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 328..365
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 630 AA; 66083 MW; 96F1873B533A3E3D CRC64;
MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS
VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP AAAAAKDVNV PDIGSDEVEV
TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KVTVGDKVST GSLIMVFEVA
GEAGAAAPAA KQEAAPAAAP APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT
VEGDKASMEV PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA
AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT GRKGRILRED
VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW
VMIPHVTHFD KTDITELEAF RKQQNEEAAK RKLDVKITPV VFIMKAVAAA LEQMPRFNSS
LSEDGQRLTL KKYINIGVAV DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA
GEMQGGCFTI SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS
FDHRVIDGAD GARFITIINN TLSDIRRLVM
//