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Database: UniProt/TrEMBL
Entry: A7GRZ7_BACCN
LinkDB: A7GRZ7_BACCN
Original site: A7GRZ7_BACCN 
ID   A7GRZ7_BACCN            Unreviewed;       470 AA.
AC   A7GRZ7;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   14-MAY-2014, entry version 55.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
GN   OrderedLocusNames=Bcer98_2671;
OS   Bacillus cereus subsp. cytotoxis (strain NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA   Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.H.,
RA   Sanchis V., Nguen-The C., Lereclus D., Richardson P., Wincker P.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS22905.1; -; Genomic_DNA.
DR   RefSeq; YP_001375900.1; NC_009674.1.
DR   ProteinModelPortal; A7GRZ7; -.
DR   SMR; A7GRZ7; 8-462.
DR   STRING; 315749.Bcer98_2671; -.
DR   EnsemblBacteria; ABS22905; ABS22905; Bcer98_2671.
DR   GeneID; 5347409; -.
DR   KEGG; bcy:Bcer98_2671; -.
DR   PATRIC; 18933952; VBIBacCyt128034_2820.
DR   eggNOG; COG1249; -.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   OMA; FANFGTE; -.
DR   OrthoDB; EOG6QCD6D; -.
DR   BioCyc; BCYT315749:GH2A-2779-MONOMER; -.
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   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   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; SSF55424; 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;
KW   Redox-active center.
SQ   SEQUENCE   470 AA;  49355 MW;  1F314D1DE47F7053 CRC64;
     MVVGDFPIEL DTVVVGAGPG GYVAAIRAAQ LGQKVAVIEK ANLGGVCLNV GCIPSKALIN
     AGHRFEHAKH SDDMGIIAEN VTVDFTKVQE WKNGVVKKLT GGVEGLLKGN KVEIIRGEAY
     FVDANTLRVM TEDAAQTYTF KNAILATGST PIEIPGFKYS KRVINSTGAL SLPEIPKKLV
     VIGGGYIGME LGTAYANFGT EVTVVEAGDE ILAGFEKAMS SVVKRALQKK GNVTIHTKAM
     AKGVEETENG VKVSFEVKGE VQTVEADYVL VTVGRRPNTQ EIGLEQLGIK MTDRGLIEID
     EQCRTNVPNI YAIGDIVPGP PLAHKASYEG KVAAEAISGH AAAIDYIGIP AVCFTDPELA
     SVGYTKKQAE EAGMSVAVSK FPFAANGRAL SLNSTDGFLQ LVTRKEDGLL VGAQVAGAGA
     SDIISELGLA IEAGMTAEDI AQTIHAHPTL GEITMEAAEV ALGMPIHIVK
//
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