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ODP1_ECO57
ID   ODP1_ECO57              Reviewed;         887 AA.
AC   P0AFG9; P06958; P78049; Q53382;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            Short=PDH E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; OrderedLocusNames=Z0124, ECs0118;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC       catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC         acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Part of the PDH complex, consisting of multiple
CC       copies of pyruvate dehydrogenase (E1), dihydrolipoamide
CC       acetyltransferase (E2) and lipoamide dehydrogenase (E3). {ECO:0000250}.
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DR   EMBL; AE005174; AAG54418.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33541.1; -; Genomic_DNA.
DR   PIR; F85494; F85494.
DR   PIR; F90643; F90643.
DR   RefSeq; NP_308145.1; NC_002695.1.
DR   RefSeq; WP_000003820.1; NZ_SWKA01000005.1.
DR   PDB; 3LPL; X-ray; 2.10 A; A/B=2-887.
DR   PDB; 3LQ2; X-ray; 1.96 A; A/B=2-887.
DR   PDB; 3LQ4; X-ray; 1.98 A; A/B=2-887.
DR   PDBsum; 3LPL; -.
DR   PDBsum; 3LQ2; -.
DR   PDBsum; 3LQ4; -.
DR   AlphaFoldDB; P0AFG9; -.
DR   SMR; P0AFG9; -.
DR   IntAct; P0AFG9; 3.
DR   STRING; 155864.EDL933_0116; -.
DR   EnsemblBacteria; AAG54418; AAG54418; Z0124.
DR   EnsemblBacteria; BAB33541; BAB33541; ECs_0118.
DR   GeneID; 66671598; -.
DR   GeneID; 913657; -.
DR   KEGG; ece:Z0124; -.
DR   KEGG; ecs:ECs_0118; -.
DR   PATRIC; fig|386585.9.peg.216; -.
DR   eggNOG; COG2609; Bacteria.
DR   HOGENOM; CLU_009154_2_0_6; -.
DR   OMA; PDEYRTF; -.
DR   EvolutionaryTrace; P0AFG9; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR035807; PDC_E1_N.
DR   InterPro; IPR004660; PDH_E1.
DR   InterPro; IPR041621; PDH_E1_M.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43825:SF3; PTHR43825:SF3; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00759; aceE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Glycolysis; Magnesium; Metal-binding;
KW   Oxidoreductase; Pyruvate; Reference proteome; Thiamine pyrophosphate.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..887
FT                   /note="Pyruvate dehydrogenase E1 component"
FT                   /id="PRO_0000162244"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         716
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           76..99
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           109..124
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          131..133
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           145..154
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           160..163
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   TURN            185..187
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           197..214
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          225..230
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           237..240
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           243..248
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          254..260
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          265..269
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          271..273
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           275..285
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          289..293
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           297..299
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           300..305
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           310..317
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           320..326
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           331..337
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           339..341
FT                   /evidence="ECO:0007829|PDB:3LQ4"
FT   HELIX           343..346
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   TURN            347..349
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           354..357
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           363..365
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           367..379
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          385..390
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   TURN            393..396
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           416..424
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           431..434
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           447..457
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   TURN            458..460
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           479..482
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           483..486
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           495..506
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   TURN            510..515
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          516..522
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           525..527
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           530..536
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          565..567
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           572..583
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           585..588
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          594..600
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           601..603
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           605..617
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          623..628
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   TURN            631..633
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   TURN            635..637
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   TURN            639..641
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           646..650
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          656..659
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           664..679
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          687..691
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           707..712
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          714..720
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          726..731
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           733..735
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           736..750
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          753..760
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           762..778
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           788..792
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          798..801
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           807..810
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           811..815
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   STRAND          817..819
FT                   /evidence="ECO:0007829|PDB:3LQ4"
FT   STRAND          821..824
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           835..841
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           846..859
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   HELIX           865..874
FT                   /evidence="ECO:0007829|PDB:3LQ2"
FT   TURN            884..886
FT                   /evidence="ECO:0007829|PDB:3LQ2"
SQ   SEQUENCE   887 AA;  99668 MW;  7FB3811DE11BDD02 CRC64;
     MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY
     INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV
     CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH
     PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK
     GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD
     ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL
     NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH
     IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ
     DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS
     PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY
     SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD
     PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI
     EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP
     LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH
     HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA
 
 
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