(data stored in SCRATCH zone)

SWISSPROT: DLDH2_BACSU

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   11-DEC-2019, entry version 150.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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).
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).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=M97391; Type=Frameshift; Evidence={ECO:0000305};
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; NP_390286.2; NC_000964.3.
DR   RefSeq; WP_003230317.1; NC_000964.3.
DR   SMR; P54533; -.
DR   STRING; 224308.BSU24060; -.
DR   jPOST; P54533; -.
DR   PaxDb; P54533; -.
DR   PRIDE; P54533; -.
DR   EnsemblBacteria; CAB14337; CAB14337; BSU24060.
DR   GeneID; 938669; -.
DR   KEGG; bsu:BSU24060; -.
DR   PATRIC; fig|224308.179.peg.2620; -.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276708; -.
DR   InParanoid; P54533; -.
DR   KO; K00382; -.
DR   OMA; YFKGNSK; -.
DR   PhylomeDB; P54533; -.
DR   BioCyc; BSUB:BSU24060-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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;
DR   PRODOM; P54533.
DR   SWISS-2DPAGE; P54533.
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD;
KW   Oxidoreductase; Redox-active center; Reference proteome.
FT   CHAIN           1..474
FT                   /note="Dihydrolipoyl dehydrogenase"
FT                   /id="PRO_0000068017"
FT   NP_BIND         34..42
FT                   /note="FAD"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         188..192
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         278..281
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        453
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /note="FAD"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /note="FAD; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /note="NAD; via amide nitrogen"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /note="FAD"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /note="FAD; via amide nitrogen"
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..47
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
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
//

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