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 01-MAY-2013, entry version 147.
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; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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.
RT Nucleotide sequence encoding the dihydrolipoamide acetyltransferase
RT 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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(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
RT MG1655 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
RT in the genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP PROTEIN SEQUENCE OF 35-47.
RX PubMed=6821375;
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;
RA Russel G.C., Guest J.R.;
RT "Overexpression of restructured pyruvate dehydrogenase complexes and
RT site-directed mutagenesis of a potential active-site histidine
RT residue.";
RL Biochem. J. 269:443-450(1990).
RN [7]
RP LIPOYLATED DOMAINS STUDIES.
RX PubMed=2121129;
RA Ali S.T., Guest J.R.;
RT "Isolation and characterization of lipoylated and unlipoylated domains
RT of the E2p subunit of the pyruvate dehydrogenase complex of
RT Escherichia 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.,
RA 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 MASS 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
CC multiple copies of three enzymatic components: pyruvate
CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC lipoamide dehydrogenase (E3).
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC -!- COFACTOR: Binds 3 lipoyl cofactors covalently.
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry.
CC -!- INTERACTION:
CC P0AED9:dcm; NbExp=2; IntAct=EBI-542707, EBI-548525;
CC P32053:intA; NbExp=2; IntAct=EBI-542707, EBI-552967;
CC P0A9P0:lpdA; NbExp=2; IntAct=EBI-542707, EBI-542856;
CC P0ADI0:pinR; NbExp=2; IntAct=EBI-542707, EBI-544672;
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC -!- SIMILARITY: Contains 3 lipoyl-binding domains.
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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_000913.2.
DR RefSeq; YP_488418.1; NC_007779.1.
DR PDB; 1QJO; NMR; -; A=206-284.
DR PDB; 2K7V; NMR; -; A/B=219-293.
DR PDBsum; 1QJO; -.
DR PDBsum; 2K7V; -.
DR ProteinModelPortal; P06959; -.
DR SMR; P06959; 1-81, 106-183, 206-284, 326-363, 388-630.
DR DIP; DIP-9040N; -.
DR IntAct; P06959; 84.
DR MINT; MINT-1311573; -.
DR STRING; 511145.b0115; -.
DR SWISS-2DPAGE; P06959; -.
DR PaxDb; P06959; -.
DR PRIDE; P06959; -.
DR EnsemblBacteria; AAC73226; AAC73226; b0115.
DR EnsemblBacteria; BAB96685; BAB96685; BAB96685.
DR GeneID; 12932377; -.
DR GeneID; 944794; -.
DR KEGG; ecj:Y75_p0112; -.
DR KEGG; eco:b0115; -.
DR PATRIC; 32115331; VBIEscCol129921_0117.
DR EchoBASE; EB0024; -.
DR EcoGene; EG10025; aceF.
DR eggNOG; COG0508; -.
DR HOGENOM; HOG000281562; -.
DR KO; K00627; -.
DR OMA; VPMTRLM; -.
DR ProtClustDB; PRK11854; -.
DR BioCyc; EcoCyc:E2P-MONOMER; -.
DR BioCyc; ECOL316407:JW0111-MONOMER; -.
DR BioCyc; MetaCyc:E2P-MONOMER; -.
DR EvolutionaryTrace; P06959; -.
DR Genevestigator; P06959; -.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:EcoliWiki.
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:glycolysis; 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.
DR InterPro; IPR004167; E3-bd.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 3.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; E3_bd; 1.
DR SUPFAM; SSF51230; Hybrid_motif; 3.
DR TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Complete proteome;
KW Direct protein sequencing; Glycolysis; Lipoyl; Reference proteome;
KW Repeat; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 630 Dihydrolipoyllysine-residue
FT acetyltransferase component of pyruvate
FT dehydrogenase complex.
FT /FTId=PRO_0000162278.
FT DOMAIN 2 74 Lipoyl-binding 1.
FT DOMAIN 106 177 Lipoyl-binding 2.
FT DOMAIN 207 278 Lipoyl-binding 3.
FT REGION 317 630 Subunit binding, catalytic.
FT REGION 373 389 Hydrophobic.
FT REGION 542 567 Hydrophobic.
FT ACT_SITE 547 547 Potential.
FT ACT_SITE 603 603
FT ACT_SITE 607 607 Potential.
FT MOD_RES 41 41 N6-lipoyllysine.
FT MOD_RES 144 144 N6-lipoyllysine.
FT MOD_RES 245 245 N6-lipoyllysine.
FT MOD_RES 396 396 N6-acetyllysine.
FT MUTAGEN 603 603 H->C: Abolishes catalytic activity.
FT STRAND 206 209
FT STRAND 215 217
FT STRAND 219 223
FT STRAND 227 229
FT STRAND 236 246
FT STRAND 248 254
FT STRAND 256 260
FT STRAND 276 280
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
//
