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Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase)

 DLDH_THESS              Reviewed;         461 AA.
P85207; A9JPS7; E8PKA3;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
22-NOV-2017, entry version 65.
RecName: Full=Dihydrolipoyl dehydrogenase;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
Name=lpd {ECO:0000312|EMBL:CAO77701.1}; Synonyms=lpdA1;
OrderedLocusNames=TSC_c02350;
Thermus scotoductus (strain ATCC 700910 / SA-01).
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
Thermus.
NCBI_TaxID=743525;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION,
COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 700910 / SA-01;
PubMed=18218019; DOI=10.1111/j.1574-6968.2007.01063.x;
Opperman D.J., van Heerden E.;
"A membrane-associated protein with Cr(VI)-reducing activity from
Thermus scotoductus SA-01.";
FEMS Microbiol. Lett. 280:210-218(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700910 / SA-01;
Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
Gottschalk G., van Heerden E., Litthauer D.;
"The genome sequence of Thermus scotoductus SA-01.";
Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Has chromate reductase activity.
{ECO:0000269|PubMed:18218019}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
{ECO:0000250|UniProtKB:P11959}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:18218019};
Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:18218019};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=55.46 uM for Cr(VI) {ECO:0000269|PubMed:18218019};
Vmax=2.262 umol/min/mg enzyme toward Cr(VI)
{ECO:0000269|PubMed:18218019};
pH dependence:
Optimum pH is 6.5. {ECO:0000269|PubMed:18218019};
Temperature dependence:
Optimum temperature is 65 degrees Celsius.
{ECO:0000269|PubMed:18218019};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11959}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18218019};
Peripheral membrane protein {ECO:0000269|PubMed:18218019}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
{ECO:0000250|UniProtKB:P11959}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=CAO77701.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AM749392; CAO77701.1; ALT_INIT; Genomic_DNA.
EMBL; CP001962; ADW20875.1; -; Genomic_DNA.
RefSeq; WP_015716160.1; NC_014974.1.
ProteinModelPortal; P85207; -.
SMR; P85207; -.
STRING; 743525.TSC_c02350; -.
EnsemblBacteria; ADW20875; ADW20875; TSC_c02350.
KEGG; tsc:TSC_c02350; -.
eggNOG; ENOG4107QN2; Bacteria.
eggNOG; COG1249; LUCA.
HOGENOM; HOG000276708; -.
KO; K00382; -.
OrthoDB; POG091H0239; -.
SABIO-RK; P85207; -.
Proteomes; UP000008087; Chromosome.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond; FAD;
Flavoprotein; Glycolysis; Membrane; NAD; Oxidoreductase;
Redox-active center; Reference proteome.
CHAIN 1 461 Dihydrolipoyl dehydrogenase.
/FTId=PRO_0000315941.
NP_BIND 33 41 FAD. {ECO:0000250|UniProtKB:P11959}.
NP_BIND 173 177 NAD. {ECO:0000250}.
NP_BIND 263 266 NAD. {ECO:0000250}.
ACT_SITE 437 437 Proton acceptor.
{ECO:0000250|UniProtKB:P11959}.
BINDING 50 50 FAD. {ECO:0000250}.
BINDING 112 112 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 196 196 NAD. {ECO:0000250}.
BINDING 306 306 FAD. {ECO:0000250}.
BINDING 314 314 FAD; via amide nitrogen. {ECO:0000250}.
DISULFID 41 46 Redox-active.
{ECO:0000250|UniProtKB:P11959}.
SEQUENCE 461 AA; 48505 MW; 3B4A1719A22BF200 CRC64;
MKTYDLIVIG TGPGGYPAAI RGAQLGLKVL AVEAAEVGGV CLNVGCIPTK ALLHAAETVH
HLKGAEGFGL KAKPELDLKK LGAWRDGVVK KLTGGVAGLL KGNKVELLRG FARFKGPREI
EVNGETYGAQ SFIIATGSEP MPLKGFPFGE DVWDSTRALR VEEGIPKRLL VIGGGAVGLE
LGQIYHRLGS EVTLIEYMPE ILPAGDRETA ALLRKALEKE GLKVRTGTKA VGYEKKQDGL
HVLLEAAQGG SQEEIVVDKI LVAVGRRPRT EGLGLEKAGV KVDERGFIQV NARMETSAPG
VYAIGDVARP PLLAHKAMKE GLVAAENAAG KNALFDFQVP SVVYTGPEWA GVGLTEEEAR
KAGYNVKVGK FPFSASGRAL TLGGAEGLIK VVGDAETDLL LGVFVVGPQA GELIAEATLA
LEMGATVSDL GLTIHPHPTL SEGLMEAAEA LHKQAIHILN R


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