DLDH_VIBPA
ID DLDH_VIBPA Reviewed; 475 AA.
AC O50286;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=E3 component of 2-oxoglutarate dehydrogenase complex;
GN Name=lpd; OrderedLocusNames=VP2517;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BB22;
RX PubMed=9620967; DOI=10.1128/jb.180.12.3166-3173.1998;
RA McCarter L.L.;
RT "OpaR, a homolog of Vibrio harveyi LuxR, controls opacity of Vibrio
RT parahaemolyticus.";
RL J. Bacteriol. 180:3166-3173(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC contains multiple copies of 3 enzymatic components: branched-chain
CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AF035967; AAC46405.1; -; Genomic_DNA.
DR EMBL; BA000031; BAC60780.1; -; Genomic_DNA.
DR RefSeq; NP_798896.1; NC_004603.1.
DR RefSeq; WP_005479684.1; NC_004603.1.
DR AlphaFoldDB; O50286; -.
DR SMR; O50286; -.
DR STRING; 223926.28807515; -.
DR PRIDE; O50286; -.
DR EnsemblBacteria; BAC60780; BAC60780; BAC60780.
DR GeneID; 1190032; -.
DR KEGG; vpa:VP2517; -.
DR PATRIC; fig|223926.6.peg.2414; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_1_6; -.
DR OMA; HMVGDRM; -.
DR Proteomes; UP000002493; Chromosome 1.
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..475
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068053"
FT ACT_SITE 445
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 36..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 182..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 45..50
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 160
FT /note="P -> S (in Ref. 1; AAC46405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 50988 MW; 67F6E3A8C28DFB44 CRC64;
MSKEIKAQVV VLGSGPAGYS AAFRCADLGL ETVLVERYST LGGVCLNVGC IPSKALLHVS
KVIEEAKAMA DHGVVFGEPQ TDINKIRIWK EKVVNQLTGG LSGMAKMRNV TVVNGYGKFT
GPNSILVEGE GESTVVNFDN AIVAAGSRPI KLPFIPHEDP RIWDSTDALE LKEVPEKLLI
MGGGIIGLEM GTVYHSLGSK VEVVEMFDQV IPAADKDIVK VYTKRIKDKF KLMLETKVTA
VEAKEDGIYV SMEGKKAPAE AERYDAVLVA IGRVPNGKLI DGEKAGLEID ERGFINVDKQ
MRTNVPHIFA IGDIVGQPML AHKGVHEGHV AAEVISGKKH YFDPKVIPSI AYTEPEVAWV
GKTEKEAKAE GIKYEVATFP WAASGRAIAS DCSDGMTKLI FDKETHRVIG GAIVGTNGGE
LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GSITDLPNKK AVKKK
