(data stored in ACNUC7421 zone)

SWISSPROT: DLDH_ECO57

ID   DLDH_ECO57              Reviewed;         474 AA.
AC   P0A9P2; P00391;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-JUL-2017, entry version 91.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   AltName: Full=E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes;
DE   AltName: Full=Glycine cleavage system L protein;
GN   Name=lpdA; OrderedLocusNames=Z0126, ECs0120;
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
CC       cleavage system as well as of the alpha-ketoacid dehydrogenase
CC       complexes. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC       protein N(6)-(lipoyl)lysine + NADH.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
DR   EMBL; AE005174; AAG54420.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33543.1; -; Genomic_DNA.
DR   PIR; H85494; H85494.
DR   PIR; H90643; H90643.
DR   RefSeq; NP_308147.1; NC_002695.1.
DR   RefSeq; WP_000102485.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; P0A9P2; -.
DR   SMR; P0A9P2; -.
DR   STRING; 155864.Z0126; -.
DR   PRIDE; P0A9P2; -.
DR   EnsemblBacteria; AAG54420; AAG54420; Z0126.
DR   EnsemblBacteria; BAB33543; BAB33543; BAB33543.
DR   GeneID; 913660; -.
DR   KEGG; ece:Z0126; -.
DR   KEGG; ecs:ECs0120; -.
DR   PATRIC; fig|386585.9.peg.218; -.
DR   eggNOG; ENOG4107QN2; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0A9P2.
DR   SWISS-2DPAGE; P0A9P2.
KW   Acetylation; Complete proteome; Cytoplasm; Disulfide bond; FAD;
KW   Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    474       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068028.
FT   NP_BIND      36     45       FAD. {ECO:0000250}.
FT   NP_BIND     182    186       NAD. {ECO:0000250}.
FT   NP_BIND     270    273       NAD. {ECO:0000250}.
FT   ACT_SITE    445    445       Proton acceptor. {ECO:0000250}.
FT   BINDING      54     54       FAD. {ECO:0000250}.
FT   BINDING     117    117       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING     205    205       NAD. {ECO:0000250}.
FT   BINDING     238    238       NAD; via amide nitrogen. {ECO:0000250}.
FT   BINDING     313    313       FAD. {ECO:0000250}.
FT   BINDING     321    321       FAD; via amide nitrogen. {ECO:0000250}.
FT   MOD_RES     220    220       N6-acetyllysine. {ECO:0000250}.
FT   DISULFID     45     50       Redox-active. {ECO:0000250}.
SQ   SEQUENCE   474 AA;  50688 MW;  ED16149A3BDF333A CRC64;
     MSTEIKTQVV VLGAGPAGYS AAFRCADLGL ETVIVERYNT LGGVCLNVGC IPSKALLHVA
     KVIEEAKALA EHGIVFGEPK TDIDKIRTWK EKVINQLTGG LAGMAKGRKV KVVNGLGKFT
     GANTLEVEGE NGKTVINFDN AIIAAGSRPI QLPFIPHEDP RIWDSTDALE LKEVPERLLV
     MGGGIIGLEM GTVYHALGSQ IDVVEMFDQV IPAADKDIVK VFTKRISKKF NLMLETKVTA
     VEAKEDGIYV TMEGKKAPAE PQRYDAVLVA IGRVPNGKNL DAGKAGVEVD DRGFIRVDKQ
     LRTNVPHIFA IGDIVGQPML AHKGVHEGHV AAEVIAGKKH YFDPKVIPSI AYTEPEVAWV
     GLTEKEAKEK GISYETATFP WAASGRAIAS DCADGMTKLI FDKESHRVIG GAIVGTNGGE
     LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GSITDLPNPK AKKK
//

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