ID   ODP2_ECOLI              Reviewed;         630 AA.
AC   P06959;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 215.
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; OrderedLocusNames=b0115, JW0111;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND LIPOYLATION AT LYS-41; LYS-144 AND
RP   LYS-245.
RC   STRAIN=K12;
RX   PubMed=6345153; DOI=10.1111/j.1432-1033.1983.tb07490.x;
RA   Stephens P.E., Darlison M.G., Lewis H.M., Guest J.R.;
RT   "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide
RT   sequence encoding the dihydrolipoamide acetyltransferase component.";
RL   Eur. J. Biochem. 133:481-489(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-13.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [5]
RP   PROTEIN SEQUENCE OF 35-47, AND LIPOYLATION AT LYS-41.
RX   PubMed=6821375; DOI=10.1042/bj1870905;
RA   Hale G., Perham R.N.;
RT   "Amino acid sequence around lipoic acid residues in the pyruvate
RT   dehydrogenase multienzyme complex of Escherichia coli.";
RL   Biochem. J. 187:905-908(1980).
RN   [6]
RP   MUTAGENESIS OF HIS-603.
RX   PubMed=2201286; DOI=10.1042/bj2690443;
RA   Russel G.C., Guest J.R.;
RT   "Overexpression of restructured pyruvate dehydrogenase complexes and site-
RT   directed mutagenesis of a potential active-site histidine residue.";
RL   Biochem. J. 269:443-450(1990).
RN   [7]
RP   LIPOYLATED DOMAINS STUDIES, AND LIPOYLATION AT LYS-144.
RX   PubMed=2121129; DOI=10.1042/bj2710139;
RA   Ali S.T., Guest J.R.;
RT   "Isolation and characterization of lipoylated and unlipoylated domains of
RT   the E2p subunit of the pyruvate dehydrogenase complex of Escherichia
RT   coli.";
RL   Biochem. J. 271:139-145(1990).
RN   [8]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(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).
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   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC       Note=Binds 3 lipoyl cofactors covalently.;
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry.
CC   -!- INTERACTION:
CC       P06959; P04395: alkA; NbExp=2; IntAct=EBI-542707, EBI-544077;
CC       P06959; P0AED9: dcm; NbExp=3; IntAct=EBI-542707, EBI-548525;
CC       P06959; P32053: intA; NbExp=3; IntAct=EBI-542707, EBI-552967;
CC       P06959; P0A9P0: lpdA; NbExp=3; IntAct=EBI-542707, EBI-542856;
CC       P06959; P0ADI0: pinR; NbExp=3; IntAct=EBI-542707, EBI-544672;
CC       P06959; P24230: recG; NbExp=2; IntAct=EBI-542707, EBI-556882;
CC       P06959; P30014: rnt; NbExp=2; IntAct=EBI-542707, EBI-557418;
CC       P06959; P67087: rsmI; NbExp=2; IntAct=EBI-542707, EBI-561394;
CC       P06959; P07604: tyrR; NbExp=2; IntAct=EBI-542707, EBI-559274;
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; V01498; CAA24741.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73226.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96685.1; -; Genomic_DNA.
DR   PIR; A30278; XXECDP.
DR   RefSeq; NP_414657.1; NC_000913.3.
DR   RefSeq; WP_000963518.1; NZ_STEB01000010.1.
DR   PDB; 1QJO; NMR; -; A=206-284.
DR   PDB; 2K7V; NMR; -; A/B=206-293.
DR   PDB; 7B9K; EM; 3.16 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-630.
DR   PDBsum; 1QJO; -.
DR   PDBsum; 2K7V; -.
DR   PDBsum; 7B9K; -.
DR   AlphaFoldDB; P06959; -.
DR   EMDB; EMD-12104; -.
DR   SMR; P06959; -.
DR   BioGRID; 4261371; 5.
DR   BioGRID; 849195; 1.
DR   ComplexPortal; CPX-3943; Pyruvate dehydrogenase complex.
DR   DIP; DIP-9040N; -.
DR   IntAct; P06959; 86.
DR   STRING; 511145.b0115; -.
DR   iPTMnet; P06959; -.
DR   jPOST; P06959; -.
DR   PaxDb; 511145-b0115; -.
DR   EnsemblBacteria; AAC73226; AAC73226; b0115.
DR   GeneID; 66671597; -.
DR   GeneID; 944794; -.
DR   KEGG; ecj:JW0111; -.
DR   KEGG; eco:b0115; -.
DR   PATRIC; fig|1411691.4.peg.2167; -.
DR   EchoBASE; EB0024; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_6; -.
DR   InParanoid; P06959; -.
DR   OMA; MPFCIKA; -.
DR   OrthoDB; 9805770at2; -.
DR   PhylomeDB; P06959; -.
DR   BioCyc; EcoCyc:E2P-MONOMER; -.
DR   BioCyc; MetaCyc:E2P-MONOMER; -.
DR   BRENDA; 1.2.1.104; 2026.
DR   BRENDA; 1.3.1.12; 2026.
DR   BRENDA; 2.3.1.12; 2026.
DR   SABIO-RK; P06959; -.
DR   EvolutionaryTrace; P06959; -.
DR   PRO; PR:P06959; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:EcoCyc.
DR   GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IDA:EcoliWiki.
DR   GO; GO:0031405; F:lipoic acid binding; IDA:EcoliWiki.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IMP:EcoliWiki.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0042867; P:pyruvate catabolic process; NAS:ComplexPortal.
DR   GO; GO:0006090; P:pyruvate metabolic process; IMP:EcoliWiki.
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.
DR   SWISS-2DPAGE; P06959; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Direct protein sequencing;
KW   Lipoyl; Reference proteome; Repeat; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298646"
FT   CHAIN           2..630
FT                   /note="Dihydrolipoyllysine-residue acetyltransferase
FT                   component of pyruvate dehydrogenase complex"
FT                   /id="PRO_0000162278"
FT   DOMAIN          2..75
FT                   /note="Lipoyl-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          105..178
FT                   /note="Lipoyl-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          206..279
FT                   /note="Lipoyl-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          328..365
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   REGION          373..389
FT                   /note="Hydrophobic"
FT   REGION          542..567
FT                   /note="Hydrophobic"
FT   ACT_SITE        547
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        603
FT   ACT_SITE        607
FT                   /evidence="ECO:0000255"
FT   MOD_RES         41
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT                   ECO:0000269|PubMed:6345153, ECO:0000269|PubMed:6821375"
FT   MOD_RES         144
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT                   ECO:0000269|PubMed:2121129, ECO:0000269|PubMed:6345153"
FT   MOD_RES         245
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT                   ECO:0000269|PubMed:6345153"
FT   MOD_RES         396
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   MUTAGEN         603
FT                   /note="H->C: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:2201286"
FT   STRAND          206..209
FT                   /evidence="ECO:0007829|PDB:1QJO"
FT   STRAND          215..217
FT                   /evidence="ECO:0007829|PDB:1QJO"
FT   STRAND          219..224
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:2K7V"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:2K7V"
FT   STRAND          239..242
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          244..250
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          268..272
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          276..280
FT                   /evidence="ECO:0007829|PDB:1QJO"
FT   STRAND          396..398
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   HELIX           407..422
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          425..433
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   HELIX           435..450
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   HELIX           459..473
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   HELIX           475..477
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          483..485
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          496..502
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          505..507
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          510..512
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   TURN            514..516
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   HELIX           519..535
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          542..544
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          549..552
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   TURN            554..556
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          559..562
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          569..575
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          579..584
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   STRAND          586..602
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   TURN            603..605
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   HELIX           608..623
FT                   /evidence="ECO:0007829|PDB:7B9K"
FT   HELIX           625..628
FT                   /evidence="ECO:0007829|PDB:7B9K"
SQ   SEQUENCE   630 AA;  66096 MW;  802A513A1E88F5DA CRC64;
     MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS
     VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP AAAAAKDVNV PDIGSDEVEV
     TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KVNVGDKVST 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
//