ID   DLDH2_BACSU             Reviewed;         474 AA.
AC   P54533;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 175.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4 {ECO:0000250|UniProtKB:P09624};
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   AltName: Full=E3 component of branched-chain alpha-keto acid dehydrogenase complex;
DE   AltName: Full=LPD-Val;
GN   Name=bfmBC; Synonyms=yqiV; OrderedLocusNames=BSU24060;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO C-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 412-474.
RC   STRAIN=168;
RX   PubMed=8504804; DOI=10.1111/j.1432-1033.1993.tb17858.x;
RA   Wang G.-F., Kuriki T., Roy K.L., Kaneda T.;
RT   "The primary structure of branched-chain alpha-oxo acid dehydrogenase from
RT   Bacillus subtilis and its similarity to other alpha-oxo acid
RT   dehydrogenases.";
RL   Eur. J. Biochem. 213:1091-1099(1993).
RN   [5]
RP   FUNCTION.
RC   STRAIN=ATCC 7059;
RX   PubMed=4308861; DOI=10.1016/s0021-9258(18)94337-1;
RA   Namba Y., Yoshizawa K., Ejima A., Hayashi T., Kaneda T.;
RT   "Coenzyme A- and nicotinamide adenine dinucleotide-dependent branched chain
RT   alpha-keto acid dehydrogenase. I. Purification and properties of the enzyme
RT   from Bacillus subtilis.";
RL   J. Biol. Chem. 244:4437-4447(1969).
CC   -!- FUNCTION: Component of the branched-chain alpha-keto dehydrogenase
CC       complex, which catalyzes the overall conversion of alpha-keto acids
CC       derived from the branched-chain amino-acids valine, leucine and
CC       isoleucine to acyl-CoA and CO(2) (PubMed:4308861). The complex contains
CC       multiple copies of three enzymatic components: branched-chain alpha-
CC       keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (Probable). {ECO:0000269|PubMed:4308861,
CC       ECO:0000305}.
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:P09624};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P09063};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P09063};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000250|UniProtKB:P09624}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=M97391; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D84432; BAA12597.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14337.2; -; Genomic_DNA.
DR   EMBL; M97391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; D69962; D69962.
DR   RefSeq; WP_003230317.1; NC_000964.3.
DR   AlphaFoldDB; P54533; -.
DR   SMR; P54533; -.
DR   FunCoup; P54533; 439.
DR   STRING; 224308.BSU24060; -.
DR   jPOST; P54533; -.
DR   PaxDb; 224308-BSU24060; -.
DR   EnsemblBacteria; CAB14337; CAB14337; BSU_24060.
DR   GeneID; 938669; -.
DR   KEGG; bsu:BSU24060; -.
DR   PATRIC; fig|224308.179.peg.2620; -.
DR   eggNOG; COG1249; Bacteria.
DR   InParanoid; P54533; -.
DR   OrthoDB; 9800167at2; -.
DR   PhylomeDB; P54533; -.
DR   BioCyc; BSUB:BSU24060-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P54533; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase (NADH) activity; ISS:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IBA:GO_Central.
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:SF217; 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   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..474
FT                   /note="Dihydrolipoyl dehydrogenase"
FT                   /id="PRO_0000068017"
FT   ACT_SITE        453
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P09624"
FT   BINDING         41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P09063"
FT   BINDING         42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P09063"
FT   BINDING         51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P09063"
FT   BINDING         114
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P09063"
FT   BINDING         211
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P09063"
FT   BINDING         245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P09063"
FT   BINDING         281
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P09063"
FT   BINDING         320
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P09063"
FT   BINDING         328
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P09063"
FT   DISULFID        42..47
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P09624"
FT   CONFLICT        451..473
FT                   /note="HPHPTLSEAIGEAALAADGKAIH -> SPASNA (in Ref. 1;
FT                   BAA12597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   474 AA;  50436 MW;  38F5F8AFCF80D53F CRC64;
     MATEYDVVIL GGGTGGYVAA IRAAQLGLKT AVVEKEKLGG TCLHKGCIPS KALLRSAEVY
     RTAREADQFG VETAGVSLNF EKVQQRKQAV VDKLAAGVNH LMKKGKIDVY TGYGRILGPS
     IFSPLPGTIS VERGNGEEND MLIPKQVIIA TGSRPRMLPG LEVDGKSVLT SDEALQMEEL
     PQSIIIVGGG VIGIEWASML HDFGVKVTVI EYADRILPTE DLEISKEMES LLKKKGIQFI
     TGAKVLPDTM TKTSDDISIQ AEKDGETVTY SAEKMLVSIG RQANIEGIGL ENTDIVTENG
     MISVNESCQT KESHIYAIGD VIGGLQLAHV ASHEGIIAVE HFAGLNPHPL DPTLVPKCIY
     SSPEAASVGL TEDEAKANGH NVKIGKFPFM AIGKALVYGE SDGFVKIVAD RDTDDILGVH
     MIGPHVTDMI SEAGLAKVLD ATPWEVGQTI HPHPTLSEAI GEAALAADGK AIHF
//