ID A7GRZ7_BACCN Unreviewed; 470 AA.
AC A7GRZ7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 01-MAY-2013, entry version 49.
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; GFEKQMS; -.
DR ProtClustDB; PRK06416; -.
DR BioCyc; BCYT315749:GH2A-2813-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;
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
//
