DLDH2_HALMA
ID DLDH2_HALMA Reviewed; 472 AA.
AC Q5UYG6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Dihydrolipoyl dehydrogenase 2;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase 2;
GN Name=lpdA2; OrderedLocusNames=rrnAC2953;
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; AY596297; AAV47687.1; -; Genomic_DNA.
DR RefSeq; WP_011224529.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5UYG6; -.
DR SMR; Q5UYG6; -.
DR STRING; 272569.rrnAC2953; -.
DR EnsemblBacteria; AAV47687; AAV47687; rrnAC2953.
DR GeneID; 40153781; -.
DR KEGG; hma:rrnAC2953; -.
DR PATRIC; fig|272569.17.peg.3512; -.
DR eggNOG; arCOG01068; Archaea.
DR HOGENOM; CLU_016755_0_3_2; -.
DR OMA; DAKYGEW; -.
DR Proteomes; UP000001169; Chromosome I.
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..472
FT /note="Dihydrolipoyl dehydrogenase 2"
FT /id="PRO_0000068055"
FT ACT_SITE 450
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 275..278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 326
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 472 AA; 49244 MW; 2F9E1C042C6CBEAB CRC64;
MVVGDVTTGT ELLVIGGGPG GYVAAIRGAQ LGLDTTLVER DAYGGTCLNH GCIPSKALIS
ASDVAHDARQ AESMGVFADP AVDMAGMTEW KDGVVTRLTR GVESLCKNAG VNLVEGTAEF
VDDGTVRVAH GGEGQGSESL SFEHAIVATG SRPMAVPGFE FDGEHILSSK DALALESVPE
KLLVVGAGYI GMELSTVFAK LGAEVTVVEM LDDVLPGYED DIATVVRDRA EELGIDFNFG
EAADNWEETD EGIRVQTVDE DEVVTEYNAE KCLVAVGREP VTDTLALDNI DLQTDENGVI
PTDDQCRTAF ESVFAVGDVA GEPMLAHKAM AEGEVAARAA AGEPAAFDHQ AIPAAVFTDP
EIATVGMTES EAEAAGFEPV IGQMPVRANG RALTVNEKEG FVRVVADADE EFLLGAQIVG
PEASELIAEL GLGIEMGARL EDIAGTIHTH PTLSEAVHEA AAAARGEAVH TR
