DLDH3_HALMA
ID DLDH3_HALMA Reviewed; 477 AA.
AC Q5UWH2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Dihydrolipoyl dehydrogenase 3;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase 3;
GN Name=lpdA3; OrderedLocusNames=rrnB0197;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AY596298; AAV48381.1; -; Genomic_DNA.
DR RefSeq; WP_011224953.1; NZ_CP039136.1.
DR AlphaFoldDB; Q5UWH2; -.
DR SMR; Q5UWH2; -.
DR STRING; 272569.rrnB0197; -.
DR PRIDE; Q5UWH2; -.
DR EnsemblBacteria; AAV48381; AAV48381; rrnB0197.
DR GeneID; 40151147; -.
DR KEGG; hma:rrnB0197; -.
DR PATRIC; fig|272569.17.peg.4209; -.
DR eggNOG; arCOG01068; Archaea.
DR HOGENOM; CLU_016755_0_1_2; -.
DR OMA; RIAAYAM; -.
DR Proteomes; UP000001169; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; 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 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..477
FT /note="Dihydrolipoyl dehydrogenase 3"
FT /id="PRO_0000068056"
FT ACT_SITE 454
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 39..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 186..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 279..282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 47..52
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 50121 MW; 6F17C108465077C1 CRC64;
MVVGDVTTST DVLVIGAGPG GYVAAIRAAQ LALDVTLVEK GEYGGACLNR GCIPSKALIH
GSKLASEAGQ AEELGIYADP TVALDEMINW KDGVVDQLTS GIEQLCTAAG VNLLKGTAEF
ADENKVRIIH QGEGQGSESL KFENCIIATG SRPIEIPGFG FEDERIVSSD GALNFDTVPD
ELVIVGAGYI GMELATVYSR LGSDVSVIEM LEQALPSYEE DIASIVRKRA ERLGVDFHFG
YTADSWAASD GKAVLTAVPA DEAAHDSDIE LTADRILVAV GRRPVTDTLS IDDAGVETNA
QGFIPTDSTC RTNKEHIFAV GDVAGEPMLA HKGSKEGEVA AEVIAGEPAA VDYQALPAAV
FTDPEIGTVG LTENEAANKG MTPVTGEFQF QASGRALTAN RAEGFVRIIA TKETERVIGA
QIVGPEASEL IAEIAAMIEM GAKLEDIGST VHTHPTLSEA IMEAAQNARE KAIHRRN
