DLDH_THESS
ID DLDH_THESS Reviewed; 461 AA.
AC P85207; A9JPS7; E8PKA3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
GN Name=lpd {ECO:0000312|EMBL:CAO77701.1}; Synonyms=lpdA1;
GN OrderedLocusNames=TSC_c02350;
OS Thermus scotoductus (strain ATCC 700910 / SA-01).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=743525;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700910 / SA-01;
RX PubMed=18218019; DOI=10.1111/j.1574-6968.2007.01063.x;
RA Opperman D.J., van Heerden E.;
RT "A membrane-associated protein with Cr(VI)-reducing activity from Thermus
RT scotoductus SA-01.";
RL FEMS Microbiol. Lett. 280:210-218(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01;
RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA Gottschalk G., van Heerden E., Litthauer D.;
RT "The genome sequence of Thermus scotoductus SA-01.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has chromate reductase activity.
CC {ECO:0000269|PubMed:18218019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-
CC lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045,
CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83100; EC=1.8.1.4;
CC Evidence={ECO:0000250|UniProtKB:P11959};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:18218019};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:18218019};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55.46 uM for Cr(VI) {ECO:0000269|PubMed:18218019};
CC Vmax=2.262 umol/min/mg enzyme toward Cr(VI)
CC {ECO:0000269|PubMed:18218019};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:18218019};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:18218019};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11959}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18218019};
CC Peripheral membrane protein {ECO:0000269|PubMed:18218019}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250|UniProtKB:P11959}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAO77701.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AM749392; CAO77701.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001962; ADW20875.1; -; Genomic_DNA.
DR RefSeq; WP_015716160.1; NC_014974.1.
DR AlphaFoldDB; P85207; -.
DR SMR; P85207; -.
DR STRING; 743525.TSC_c02350; -.
DR EnsemblBacteria; ADW20875; ADW20875; TSC_c02350.
DR KEGG; tsc:TSC_c02350; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_3_0; -.
DR OrthoDB; 267896at2; -.
DR SABIO-RK; P85207; -.
DR Proteomes; UP000008087; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycolysis;
KW Membrane; NAD; Oxidoreductase; Redox-active center.
FT CHAIN 1..461
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000315941"
FT ACT_SITE 437
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11959"
FT BINDING 33..41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11959"
FT BINDING 50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 173..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 263..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 41..46
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P11959"
SQ 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
