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Database: UniProt
Entry: P06959
LinkDB: P06959
Original site: P06959 
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-SEP-2014, entry version 156.
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], AND LIPOYLATION AT LYS-41; LYS-144
RP   AND 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.
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 277:1453-1462(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
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, AND LIPOYLATION AT LYS-41.
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, AND LIPOYLATION AT LYS-144.
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 IDENTIFICATION BY
RP   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=3; 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_000913.3.
DR   RefSeq; YP_488418.1; NC_007779.1.
DR   PDB; 1QJO; NMR; -; A=206-284.
DR   PDB; 2K7V; NMR; -; A/B=206-293.
DR   PDBsum; 1QJO; -.
DR   PDBsum; 2K7V; -.
DR   ProteinModelPortal; P06959; -.
DR   SMR; P06959; 1-183, 206-284, 328-365, 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; TEIMVAV; -.
DR   OrthoDB; EOG610413; -.
DR   PhylomeDB; P06959; -.
DR   BioCyc; EcoCyc:E2P-MONOMER; -.
DR   BioCyc; ECOL316407:JW0111-MONOMER; -.
DR   BioCyc; MetaCyc:E2P-MONOMER; -.
DR   EvolutionaryTrace; P06959; -.
DR   PRO; PR:P06959; -.
DR   Genevestigator; P06959; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0005515; F:protein binding; IPI:IntAct.
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:0055114; P:oxidation-reduction process; IDA:GOC.
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.
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; 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.
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
//
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