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 03-AUG-2022, entry version 135.
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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-
CC methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-
CC N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 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.
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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 AlphaFoldDB; P37941; -.
DR SMR; P37941; -.
DR IntAct; P37941; 2.
DR STRING; 224308.BSU24040; -.
DR jPOST; P37941; -.
DR PaxDb; P37941; -.
DR PRIDE; P37941; -.
DR EnsemblBacteria; CAB14335; CAB14335; BSU_24040.
DR GeneID; 938672; -.
DR KEGG; bsu:BSU24040; -.
DR PATRIC; fig|224308.179.peg.2618; -.
DR eggNOG; COG0022; Bacteria.
DR InParanoid; P37941; -.
DR OMA; SEAYYMA; -.
DR PhylomeDB; P37941; -.
DR BioCyc; BSUB:BSU24040-MON; -.
DR BioCyc; MetaCyc:MON-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: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;
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 ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 58..60
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 83..86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86..89
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="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
