(data stored in SCRATCH zone)

SWISSPROT: ODBA_BACSU

ID   ODBA_BACSU              Reviewed;         330 AA.
AC   P37940;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 123.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha;
DE            EC=1.2.4.4;
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain;
DE            Short=BCKDH E1-alpha;
GN   Name=bfmBAA; Synonyms=bfmB1a; OrderedLocusNames=BSU24050;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-22.
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   [2]
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   [3]
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).
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 three enzymatic components: branched-chain
CC       alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC       lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-
CC         methylpropanoyl)transferase]-(R)-N(6)-lipoyl-L-lysine + H(+) =
CC         [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-(R)-
CC         N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysine + CO2;
CC         Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. Directly
CC       associated with ODBB in the E1 complex.
CC   -!- SIMILARITY: Belongs to the BCKDHA family. {ECO:0000305}.
DR   EMBL; M97391; AAA22278.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12598.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14336.1; -; Genomic_DNA.
DR   PIR; C69593; C69593.
DR   RefSeq; NP_390285.1; NC_000964.3.
DR   RefSeq; WP_004398565.1; NZ_CM000487.1.
DR   SMR; P37940; -.
DR   STRING; 224308.BSU24050; -.
DR   PaxDb; P37940; -.
DR   PRIDE; P37940; -.
DR   EnsemblBacteria; CAB14336; CAB14336; BSU24050.
DR   GeneID; 938674; -.
DR   KEGG; bsu:BSU24050; -.
DR   PATRIC; fig|224308.179.peg.2619; -.
DR   eggNOG; COG1071; LUCA.
DR   HOGENOM; HOG000281335; -.
DR   InParanoid; P37940; -.
DR   KO; K00166; -.
DR   OMA; WHCGYDP; -.
DR   PhylomeDB; P37940; -.
DR   BioCyc; BSUB:BSU24050-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-11683; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003826; F:alpha-ketoacid dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; IBA:GO_Central.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37940.
DR   SWISS-2DPAGE; P37940.
KW   Direct protein sequencing; Magnesium; Metal-binding; Oxidoreductase;
KW   Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..330
FT                   /note="2-oxoisovalerate dehydrogenase subunit alpha"
FT                   /id="PRO_0000162248"
FT   REGION          72..74
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          107..110
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          123..125
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          153..159
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          183..187
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   METAL           154
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           183
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           185
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   330 AA;  36334 MW;  39584D3F4363E656 CRC64;
     MSTNRHQALG LTDQEAVDMY RTMLLARKID ERMWLLNRSG KIPFVISCQG QEAAQVGAAF
     ALDREMDYVL PYYRDMGVVL AFGMTAKDLM MSGFAKAADP NSGGRQMPGH FGQKKNRIVT
     GSSPVTTQVP HAVGIALAGR MEKKDIAAFV TFGEGSSNQG DFHEGANFAA VHKLPVIFMC
     ENNKYAISVP YDKQVACENI SDRAIGYGMP GVTVNGNDPL EVYQAVKEAR ERARRGEGPT
     LIETISYRLT PHSSDDDDSS YRGREEVEEA KKSDPLLTYQ AYLKETGLLS DEIEQTMLDE
     IMAIVNEATD EAENAPYAAP ESALDYVYAK
//

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