(data stored in ACNUC7421 zone)

HOGENOM: BURMS_1_PE1010

ID   BURMS_1_PE1010                       STANDARD;      PRT;   466 AA.
AC   BURMS_1_PE1010; A1UXC9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Dihydrolipoyl dehydrogenase; EC=1.8.1 4; (BURMS_1.PE1010).
GN   OrderedLocusNames=BMASAVP1_1033;
OS   BURKHOLDERIA MALLEI SAVP1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320388;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BURMS_1.PE1010.
CC       Burkholderia mallei SAVP1 chromosome II, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A1UXC9_BURMS
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.
CC   -!- GENE_FAMILY: HOG000276708 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A1UXC9; -.
DR   EMBL; CP000525; ABM49268.1; -; Genomic_DNA.
DR   RefSeq; YP_990632.1; NC_008784.1.
DR   ProteinModelPortal; A1UXC9; -.
DR   SMR; A1UXC9; 4-466.
DR   STRING; A1UXC9; -.
DR   GeneID; 4677193; -.
DR   GenomeReviews; CP000525_GR; BMASAVP1_1033.
DR   KEGG; bmv:BMASAVP1_1033; -.
DR   TIGR; BMASAVP1_1033; -.
DR   OMA; YKAMPAV; -.
DR   ProtClustDB; PRK05976; -.
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   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   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   PANTHER; PTHR22912:SF20; Lipoamide_DH; 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.
DR   HOGENOMDNA; BURMS_1.PE1010; -.
KW   dihydrolipoamide dehydrogenase;
KW   Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Redox-active center.
SQ   SEQUENCE   466 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDTKTTTLL VIGGGPGGYV AAIRAGQLGV RTILVERDRL GGTCLNIGCI PSKALIHAAG
     EFDKVRGFAG DSPLGIRTQA PAIDIARTVA WKDGIVKKLT GGVGALLKKN GVEVVHGDAR
     VVDGKTVDVD TGGGARVRIQ CEHLLLAAGS EPVELPAMPF GGNVISSTGA LSPGRLPKRL
     VVVGAGYIGL ELGIAYRKLG VEVSVVEARE RILPIYDAEL TKPVAASLKR LGVRVLLGHK
     VLGLNARGDA VCVQDDAHAQ TELAADQVLV TVGRRPRTQG WGLETLQLDR AGAALKVDDM
     CRTSMRNVWA IGDLTGEPML AHRAMAQGEM VAEIVAGKKR HFMPAAIAAI CFTDPEVVSA
     GLAPDEAERT FGACVSASFP FAANGRALTL ESADGFVRVV ARRDDHLIVG WQAVGAGVSE
     LAAAFSQSLE MGARLEDVGG TIHAHPTLGE AVMEAALRAL GHALHI
//

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