(data stored in SCRATCH zone)

SWISSPROT: B7UIG4_ECO27

ID   B7UIG4_ECO27            Unreviewed;       474 AA.
AC   B7UIG4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   Name=lpd {ECO:0000313|EMBL:CAS07667.1};
GN   OrderedLocusNames=E2348C_0119 {ECO:0000313|EMBL:CAS07667.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07667.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07667.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-
CC         N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH;
CC         Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-
CC         COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100;
CC         EC=1.8.1.4; Evidence={ECO:0000256|RuleBase:RU003692};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3,
CC         ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3,
CC       ECO:0000256|RuleBase:RU003692};
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000256|RuleBase:RU003692}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003692}.
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DR   EMBL; FM180568; CAS07667.1; -; Genomic_DNA.
DR   RefSeq; WP_000102485.1; NC_011601.1.
DR   SMR; B7UIG4; -.
DR   EnsemblBacteria; CAS07667; CAS07667; E2348C_0119.
DR   KEGG; ecg:E2348C_0119; -.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   OMA; TMSEAVM; -.
DR   BioCyc; ECOL574521:E2348C_RS00615-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
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   PIRSF; PIRSF000350; Mercury_reductase_MerA; 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; B7UIG4.
DR   SWISS-2DPAGE; B7UIG4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003692};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003692};
KW   Redox-active center {ECO:0000256|RuleBase:RU003692}.
FT   DOMAIN        8    328       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      347    455       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     182    189       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   NP_BIND     319    322       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    445    445       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING      54     54       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     117    117       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000350-
FT                                3}.
FT   BINDING     205    205       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     272    272       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     313    313       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     45     50       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
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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