(data stored in ACNUC7421 zone)

SWISSPROT: A1AZG9_PARDP

ID   A1AZG9_PARDP            Unreviewed;       464 AA.
AC   A1AZG9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 93.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   OrderedLocusNames=Pden_0551 {ECO:0000313|EMBL:ABL68663.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68663.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000489; ABL68663.1; -; Genomic_DNA.
DR   RefSeq; WP_011746896.1; NC_008686.1.
DR   STRING; 318586.Pden_0551; -.
DR   PRIDE; A1AZG9; -.
DR   EnsemblBacteria; ABL68663; ABL68663; Pden_0551.
DR   KEGG; pde:Pden_0551; -.
DR   eggNOG; ENOG4107QN2; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   OMA; YFKGNSK; -.
DR   BioCyc; PDEN318586:G1GW1-554-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; A1AZG9.
DR   SWISS-2DPAGE; A1AZG9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
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   ECO:0000313|EMBL:ABL68663.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU003692};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT   DOMAIN        4    326       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      345    454       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     139    141       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   NP_BIND     178    185       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   NP_BIND     317    320       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    443    443       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING      51     51       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     201    201       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     270    270       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     311    311       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     42     47       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   464 AA;  48820 MW;  DF5A51FB9868EF3A CRC64;
     MSTYDLIVIG AGPGGYVCAI RAAQLGLKVA CVEGRETLGG TCLNVGCIPS KALLHASHML
     HETHENFEKM GLMGAKPKVD WGKMQGYKAE TVGGNTKGIE FLFKKNKIDW LKGWASIEAP
     GKVKVGDTTH ETKNIVIATG SEPASLKGVE VDNDAGIVVD STGALSLPKI PKSMVVIGAG
     VIGLELGSAY ARLGAEVTVV EFLDAITPGM DGEVQKQFQR ILAKQGLKFV LGAAVSGVEV
     EKGKAEVKYK LRKDDSEHEI KAECVLVATG RRPYVAGLGL DKVGVALTDR GFVQIDDHWQ
     TSVKGIYAIG DAVPGPMLAH KAEDEGMAVA EVIAGKHGHV NYDVIPGVIY TTPEVASVGL
     TEEAAKESGR KIKVGKFPFM GNARAKALFQ AEGFVKMIAD AETDRVLGCH IIGPNAGEMI
     HEVCVAMEFG ASAQDIALTC HAHPTCSEAV REAALACGDG AIHA
//

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