(data stored in SCRATCH zone)

SWISSPROT: Q3IIH6_PSEHT

ID   Q3IIH6_PSEHT            Unreviewed;       475 AA.
AC   Q3IIH6;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 94.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   Name=lpd {ECO:0000313|EMBL:CAI85491.1};
GN   OrderedLocusNames=PSHAa0393 {ECO:0000313|EMBL:CAI85491.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85491.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85491.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC       protein N(6)-(lipoyl)lysine + NADH.
CC       {ECO:0000256|RuleBase:RU003692}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {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; CR954246; CAI85491.1; -; Genomic_DNA.
DR   RefSeq; WP_011327104.1; NC_007481.1.
DR   ProteinModelPortal; Q3IIH6; -.
DR   STRING; 326442.PSHAa0393; -.
DR   EnsemblBacteria; CAI85491; CAI85491; PSHAa0393.
DR   GeneID; 32565798; -.
DR   KEGG; pha:PSHAa0393; -.
DR   eggNOG; ENOG4107QN2; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   OMA; TMSEAVM; -.
DR   OrthoDB; POG091H0239; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005623; C:cell; IEA:GOC.
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   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR006258; Lipoamide_DH.
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   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; Q3IIH6.
DR   SWISS-2DPAGE; Q3IIH6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   FAD {ECO:0000256|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|RuleBase:RU003692};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003692,
KW   ECO:0000313|EMBL:CAI85491.1}; Pyruvate {ECO:0000313|EMBL:CAI85491.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU003692};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   DOMAIN        8    327       FAD/NAD-binding_dom. {ECO:0000259|Pfam:
FT                                PF07992}.
FT   DOMAIN      346    454       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
SQ   SEQUENCE   475 AA;  50122 MW;  61EFE59E819F2C25 CRC64;
     MSNELKTQVV VLGGGPGGYS AAFRAADLGL EVTLVESRDT LGGVCLNVGC IPSKALLHVA
     KVIDDAAAMA DHGVTFGAPQ IDLDKIRSWK DSVIGQLTGG LTSMSKMRKV KVVYGYGKFT
     GSNTIAVEGT DGTTTITFDN AIIAAGSKPV SLPFIPEDDR VIDSTGALEL KDIPEKLLVL
     GGGIIGLEMG TVYRALGSAI DVVEFADQLV PAADKDIVKI YQKYVSDKFN VMLSTKVTGI
     DAKDDGLYVT FEGKNAPAEP VRYDKVLVAV GRTPNGKLLD ADKAGVNVDD RGFINVDKQL
     KTNVEHIFAV GDIVGQPMLA HKAVHEAHVA AEVISGQKHY FDPKCIPSIA YTDPEMAWVG
     VTEKEAKEQG LSIETAVFPW AASGRAIASA RTEGSTKLIF DKESGRVIGG AMVGINAGEM
     LGEIGLAVEM GADGEDLALT IHAHPTLNES IGLAAEIYEG SITDLPNKKA VKKKK
//

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