ID D4IG44_ERWAE Unreviewed; 475 AA.
AC D4IG44;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 01-MAY-2013, entry version 23.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
GN Name=lpdA; OrderedLocusNames=EAM_0749;
OS Erwinia amylovora (strain ATCC 49946 / CCPPB 0273 / Ea273 / 27-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Erwinia.
OX NCBI_TaxID=716540;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49946 / CCPPB 0273 / Ea273 / 27-3;
RX PubMed=20118253; DOI=10.1128/JB.00022-10;
RA Sebaihia M., Bocsanczy A.M., Biehl B.S., Quail M.A., Perna N.T.,
RA Glasner J.D., Declerck G.A., Cartinhour S., Schneider D.J.,
RA Bentley S.D., Parkhill J., Beer S.V.;
RT "Complete genome sequence of the plant pathogen Erwinia amylovora
RT strain ATCC 49946.";
RL J. Bacteriol. 192:2020-2021(2010).
CC -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC protein N(6)-(lipoyl)lysine + NADH.
CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond
CC (By similarity).
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family.
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DR EMBL; FN666575; CBJ45424.1; -; Genomic_DNA.
DR RefSeq; YP_003537839.1; NC_013971.1.
DR ProteinModelPortal; D4IG44; -.
DR EnsemblBacteria; CBJ45424; CBJ45424; EAM_0749.
DR GeneID; 8950587; -.
DR KEGG; eay:EAM_0749; -.
DR PATRIC; 35412919; VBIErwAmy154257_0728.
DR HOGENOM; HOG000276708; -.
DR KO; K00382; -.
DR BioCyc; EAMY716540:GJAV-786-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:EC.
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 InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR InterPro; IPR006258; Lipoamide_DH.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR PANTHER; PTHR22912:SF20; PTHR22912:SF20; 1.
DR Pfam; PF00070; Pyr_redox; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF55424; FAD/NAD-linked_reductase_dimer; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase; Pyruvate;
KW Redox-active center.
SQ SEQUENCE 475 AA; 50615 MW; 3936358A4F32FF6F CRC64;
MSTEIKTQVV VLGAGPAGYS AAFRAADLGL ETVIVERYST LGGVCLNVGC IPSKALLHVA
KVIEEAKALE AHGIVFGKPQ TDIDKVRGWK EKVISQLTGG LAGMAKGRKV NVVNGLGKFT
AANTLEVTAE DGSKTTITFD NAIIAAGSRP IELPFIPHED PRVWDSTDAL ELKEVPERLL
VMGGGIIGLE MATVYHALGS QIDVVEMFDQ VIPAADKDVV KVFTKRISKQ FNLMLETKVT
AVEAKEDGIY VTMEGKKAPS EPQRYDAVLV AIGRVPNGKG LDAGKAGVEV DDRGFIRVDK
QMRTNVPHIF AIGDIVGQPM LAHKGVHEGH VAAEVISGKK HYFDPKVIPS IAYTEPEVAW
VGLTEKEAKE QGISYETSTF PWAASGRAIA SDCADGMTKL IFDKNTHRVI GGAIVGTNGG
ELLGEIGLAI EMGCDAEDIA LTIHAHPTLH ESVGLAAEIF EGSITDLPNP KAKKK
//
