ODP2_ECOLI
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 03-AUG-2022, entry version 208.
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; Proteobacteria; 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=(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;
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 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 SWISS-2DPAGE; P06959; -.
DR jPOST; P06959; -.
DR PaxDb; P06959; -.
DR PRIDE; P06959; -.
DR EnsemblBacteria; AAC73226; AAC73226; b0115.
DR EnsemblBacteria; BAB96685; BAB96685; BAB96685.
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; TMEFESF; -.
DR PhylomeDB; P06959; -.
DR BioCyc; EcoCyc:E2P-MON; -.
DR BioCyc; MetaCyc:E2P-MON; -.
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; IC:ComplexPortal.
DR GO; GO:0006090; P:pyruvate metabolic process; IMP:EcoliWiki.
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; 4.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 3.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 3.
DR TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Direct protein sequencing;
KW Glycolysis; 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
