DLDH_HALVD
ID DLDH_HALVD Reviewed; 475 AA.
AC Q04829; D4GY21;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
GN Name=lpdA; Synonyms=lpd; OrderedLocusNames=HVO_2961;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 326-348.
RX PubMed=1339281; DOI=10.1139/o92-101;
RA Vettakkorumakankav N.N., Stevenson K.J.;
RT "Dihydrolipoamide dehydrogenase from Haloferax volcanii: gene cloning,
RT complete primary structure, and comparison to other dihydrolipoamide
RT dehydrogenases.";
RL Biochem. Cell Biol. 70:656-663(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP PROTEIN SEQUENCE OF 2-49.
RX PubMed=1581034; DOI=10.1139/o92-010;
RA Vettakkorumakankav N.N., Danson M.J., Hough D.W., Stevenson K.J.,
RA Davison M., Young J.;
RT "Dihydrolipoamide dehydrogenase from the halophilic archaebacterium
RT Haloferax volcanii: characterization and N-terminal sequence.";
RL Biochem. Cell Biol. 70:70-75(1992).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; L09733; AAA72340.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE04480.1; -; Genomic_DNA.
DR PIR; A56824; A56824.
DR RefSeq; WP_004044825.1; NZ_AOHU01000104.1.
DR AlphaFoldDB; Q04829; -.
DR SMR; Q04829; -.
DR STRING; 309800.C498_17965; -.
DR EnsemblBacteria; ADE04480; ADE04480; HVO_2961.
DR GeneID; 8924221; -.
DR KEGG; hvo:HVO_2961; -.
DR eggNOG; arCOG01068; Archaea.
DR HOGENOM; CLU_016755_0_3_2; -.
DR OMA; DAKYGEW; -.
DR OrthoDB; 19112at2157; -.
DR BRENDA; 1.8.1.4; 2561.
DR SABIO-RK; Q04829; -.
DR Proteomes; UP000008243; Chromosome.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Glycolysis; NAD; Oxidoreductase; Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1581034"
FT CHAIN 2..475
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068058"
FT ACT_SITE 451
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 327
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"
FT CONFLICT 244
FT /note="S -> T (in Ref. 1; AAA72340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 49974 MW; 48FFBB56B8EAE65A CRC64;
MVVGDIATGT ELLVIGAGPG GYVAAIRAAQ NGIDTTLVEK DAYGGTCLNY GCIPSKALIT
GANLAHEAGN AEEMGIHADP VVDMSQLRDW KSGVVDQLTG GVEKLCKANG VNLVEGTARF
KDENAVRIAH GGEGQGSETI EFEHCIIATG SRVIQIPGFD FGDEPVWSSR DALEADTVPE
RLVVVGGGYI GMELSTTFAK LGADVTVVEM LDDILPGYES DVARVVRKRA EELGIDMHLG
EGASGWREED DGIMVTTETE DGEENEYRAD KVLVAVGRSP VTDTMDIENA GLEADDRGFL
SVDDRRRTDV EHIYAVGDVV EDTPMLAHVA SKEGIVAAEH VAGEPVAFDS QAVPAAVFTD
PEIGTVGMTE ADAEEAGFTP VVGQMPFRAS GRALTTNHAD GFVRVVADEE SGFVLGAQIV
GPEASELIAE LAFAIEMGAT LEDVASTIHT HPTLAEAVME AAENALGQAI HTLNR
