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   02-SEP-2026, entry version 98.
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; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae;
OC   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;
RX   PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA   Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA   Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA   Berenguer J., van Heerden E., Litthauer D.;
RT   "Sequence of the hyperplastic genome of the naturally competent Thermus
RT   scotoductus SA-01.";
RL   BMC Genomics 12:577-577(2011).
CC   -!- FUNCTION: Has chromate reductase activity.
CC       {ECO:0000269|PubMed:18218019}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = N(6)-
CC         [(R)-lipoyl]-L-lysyl-[protein] + NADH + H(+); 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   KEGG; tsc:TSC_c02350; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_3_0; -.
DR   SABIO-RK; P85207; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase (NADH) activity; ISS:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:TreeGrafter.
DR   FunFam; 3.30.390.30:FF:000001; Dihydrolipoyl dehydrogenase; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR050151; Class-I_Pyr_Nuc-Dis_Oxidored.
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   NCBIfam; TIGR01350; lipoamide_DH; 1.
DR   PANTHER; PTHR22912:SF160; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Membrane;
KW   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
//