(data stored in SCRATCH zone)

SWISSPROT: ODBB_BACSU

ID   ODBB_BACSU              Reviewed;         327 AA.
AC   P37941;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 125.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit beta;
DE            EC=1.2.4.4;
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain;
DE            Short=BCKDH E1-beta;
GN   Name=bfmBAB; Synonyms=bfmB1b; OrderedLocusNames=BSU24040;
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 1-32.
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 ODBA in the E1 complex.
DR   EMBL; M97391; AAA22279.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12599.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14335.1; -; Genomic_DNA.
DR   PIR; D69593; D69593.
DR   RefSeq; NP_390284.1; NC_000964.3.
DR   RefSeq; WP_004398638.1; NZ_JNCM01000036.1.
DR   SMR; P37941; -.
DR   IntAct; P37941; 2.
DR   STRING; 224308.BSU24040; -.
DR   jPOST; P37941; -.
DR   PaxDb; P37941; -.
DR   PRIDE; P37941; -.
DR   EnsemblBacteria; CAB14335; CAB14335; BSU24040.
DR   GeneID; 938672; -.
DR   KEGG; bsu:BSU24040; -.
DR   PATRIC; fig|224308.179.peg.2618; -.
DR   eggNOG; ENOG4105CPP; Bacteria.
DR   eggNOG; COG0022; LUCA.
DR   HOGENOM; HOG000281451; -.
DR   InParanoid; P37941; -.
DR   KO; K00167; -.
DR   OMA; VQERCFH; -.
DR   PhylomeDB; P37941; -.
DR   BioCyc; BSUB:BSU24040-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-11684; -.
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:0009083; P:branched-chain amino acid catabolic process; IBA:GO_Central.
DR   GO; GO:0007584; P:response to nutrient; IBA:GO_Central.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37941.
DR   SWISS-2DPAGE; P37941.
KW   Direct protein sequencing; Oxidoreductase; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..327
FT                   /note="2-oxoisovalerate dehydrogenase subunit beta"
FT                   /id="PRO_0000162250"
FT   REGION          58..60
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          83..86
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          86..89
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  35856 MW;  F19F5BF8F413EBFE CRC64;
     MSVMSYIDAI NLAMKEEMER DSRVFVLGED VGRKGGVFKA TAGLYEQFGE ERVMDTPLAE
     SAIAGVGIGA AMYGMRPIAE MQFADFIMPA VNQIISEAAK IRYRSNNDWS CPIVVRAPYG
     GGVHGALYHS QSVEAIFANQ PGLKIVMPST PYDAKGLLKA AVRDEDPVLF FEHKRAYRLI
     KGEVPADDYV LPIGKADVKR EGDDITVITY GLCVHFALQA AERLEKDGIS AHVVDLRTVY
     PLDKEAIIEA ASKTGKVLLV TEDTKEGSIM SEVAAIISEH CLFDLDAPIK RLAGPDIPAM
     PYAPTMEKYF MVNPDKVEAA MRELAEF
//

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