(data stored in SCRATCH zone)

SWISSPROT: Q13DQ1_RHOPS

ID   Q13DQ1_RHOPS            Unreviewed;       467 AA.
AC   Q13DQ1;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   OrderedLocusNames=RPD_0550 {ECO:0000313|EMBL:ABE37788.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37788.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37788.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37788.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-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; CP000283; ABE37788.1; -; Genomic_DNA.
DR   RefSeq; WP_011500975.1; NC_007958.1.
DR   STRING; 316057.RPD_0550; -.
DR   EnsemblBacteria; ABE37788; ABE37788; RPD_0550.
DR   KEGG; rpd:RPD_0550; -.
DR   eggNOG; ENOG4107QN2; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   OMA; YFKGNSK; -.
DR   OrthoDB; 267896at2; -.
DR   BioCyc; RPAL316057:RPD_RS02820-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
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; Q13DQ1.
DR   SWISS-2DPAGE; Q13DQ1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
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:ABE37788.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU003692}.
FT   DOMAIN        4    329       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      348    457       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     144    146       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   NP_BIND     181    188       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   NP_BIND     320    323       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    446    446       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING      51     51       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     115    115       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000350-
FT                                3}.
FT   BINDING     204    204       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     273    273       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     314    314       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     42     47       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   467 AA;  48726 MW;  7D72C6D883904A46 CRC64;
     MATYDLVIIG TGPGGYVCAI RAAQLGLKVA VVEKNATLGG TCLNVGCMPS KALLHASELF
     EEAGHSFAKM GIGVPAPTLD LPAMMNFKQQ GIDGNVKGVE YLMKKNKIDV LVGRGRVLGA
     GKVEVTGNDG KAQTVETKSI VIATGSDVAK LKGIAIDEKR VVSSTGALSL DKVPERLIVV
     GAGVIGLELG SVWRRLGAQV TVVEFLDRIL PGMDSEIVKQ FQRILEKQGF AFKLGAKVTG
     VDSSGAKLAV KVEAAAGGNP ETLEADVVLV AIGRVPYTEG LGLKEAGVAL DERGRVVIDN
     HFATSVKGVY AIGDVVRGPM LAHKAEDEGV AVAELLAGKA GHVNYDVIPG VVYTTPEVSS
     VGKTEEDLKQ AGIAYTVGKF PFTANGRSKV NQTTDGLVKI LADAKTDRVL GVHIVGREAG
     ELIHEAAVLM EFGGSAEDLA RTCHAHPTRS EAVKEAALAV GKRAIHM
//

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