ID   ODB2_PSEPU              Reviewed;         423 AA.
AC   P09062;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex;
DE            EC=2.3.1.168;
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase complex component E2;
DE            Short=BCKAD-E2;
DE            Short=BCKADE2;
DE   AltName: Full=Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex;
DE   AltName: Full=Dihydrolipoamide branched chain transacylase;
DE   AltName: Full=Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase;
GN   Name=bkdB;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G2;
RX   PubMed=3046941; DOI=10.1111/j.1432-1033.1988.tb14264.x;
RA   Burns G., Brown T., Hatter K., Sokatch J.R.;
RT   "Comparison of the amino acid sequences of the transacylase components of
RT   branched chain oxoacid dehydrogenase of Pseudomonas putida, and the
RT   pyruvate and 2-oxoglutarate dehydrogenases of Escherichia coli.";
RL   Eur. J. Biochem. 176:165-169(1988).
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)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-
CC         CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC         [protein] + CoA; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475,
CC         Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1.168;
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; M57613; AAA65617.1; -; Genomic_DNA.
DR   PIR; S01322; XXPS2M.
DR   RefSeq; WP_016711829.1; NZ_LKKT01000051.1.
DR   AlphaFoldDB; P09062; -.
DR   SMR; P09062; -.
DR   GeneID; 66677015; -.
DR   GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Glycolysis; Lipoyl; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..423
FT                   /note="Lipoamide acyltransferase component of branched-
FT                   chain alpha-keto acid dehydrogenase complex"
FT                   /id="PRO_0000162303"
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          137..174
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   ACT_SITE        395
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000255"
FT   MOD_RES         44
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ   SEQUENCE   423 AA;  45129 MW;  6E325F318E6D75D7 CRC64;
     MGTHVIKMPD IGEGIAQVEL VEWFVKVGDI IAEDQVVADV MTDKATVEIP SPVSGKVLAL
     GGQPGEVMAV GSELIRIEVE GSGNHVDVPQ AKPAEVPAAP VAAKPEPQKD VKPAAYQASA
     SHEAAPIVPR QPGDKPLASP AVRKRALDAG IELRYVHGSG PAGRILHEDL DAFMSKPQSA
     AGQTPNGYAR RTDSEQVPVI GLRRKIAQRM QDAKRRVAHF SYVEEIDVTA LEALRQQLNS
     KHGDSRGKLT LLPFLVRALV VALRDFPQIN ATYDDEAQII TRHGAVHVGI ATQGDNGLMV
     PVLRHAEAGS LWANAGEISR LANAARNNKA SREELSGSTI TLTSLGALGG IVSTPVVNTP
     EVAIVGVNRM VERPVVIDGQ IVVRKMMNLS SSFDHRVVDG MDAALFIQAV RGLLEQPACL
     FVE