ODB2_PSEAE
ID ODB2_PSEAE Reviewed; 428 AA.
AC Q9I1M0; Q99384;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
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; OrderedLocusNames=PA2249;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP PROTEIN SEQUENCE OF 2-22.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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) (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG05637.1; -; Genomic_DNA.
DR PIR; E83365; E83365.
DR RefSeq; NP_250939.1; NC_002516.2.
DR RefSeq; WP_003113728.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; Q9I1M0; -.
DR SMR; Q9I1M0; -.
DR STRING; 287.DR97_6301; -.
DR PaxDb; Q9I1M0; -.
DR PRIDE; Q9I1M0; -.
DR EnsemblBacteria; AAG05637; AAG05637; PA2249.
DR GeneID; 880679; -.
DR KEGG; pae:PA2249; -.
DR PATRIC; fig|208964.12.peg.2350; -.
DR PseudoCAP; PA2249; -.
DR HOGENOM; CLU_016733_10_0_6; -.
DR InParanoid; Q9I1M0; -.
DR OMA; HPCIMAP; -.
DR PhylomeDB; Q9I1M0; -.
DR BioCyc; PAER208964:G1FZ6-2288-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031405; F:lipoic acid binding; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Glycolysis; Lipoyl;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3046941"
FT CHAIN 2..428
FT /note="Lipoamide acyltransferase component of branched-
FT chain alpha-keto acid dehydrogenase complex"
FT /id="PRO_0000287785"
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 140..177
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 88..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 400
FT /evidence="ECO:0000255"
FT ACT_SITE 404
FT /evidence="ECO:0000255"
FT MOD_RES 44
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ SEQUENCE 428 AA; 45774 MW; D7B3E75901E36484 CRC64;
MGTHVIKMPD IGEGIAEVEL VEWHVQVGDS VNEDQVLAEV MTDKATVEIP SPVAGRILAL
GGQPGQVMAV GGELIRLEVE GAGNLAESPA AATPAAPVAA TPEKPKEAPV AAPKAAAEAP
RALRDSEAPR QRRQPGERPL ASPAVRQRAR DLGIELQFVQ GSGPAGRVLH EDLDAYLTQD
GSVARSGGAA QGYAERHDEQ AVPVIGLRRK IAQKMQDAKR RIPHFSYVEE IDVTDLEALR
AHLNQKWGGQ RGKLTLLPFL VRAMVVALRD FPQLNARYDD EAEVVTRYGA VHVGIATQSD
NGLMVPVLRH AESRDLWGNA SEVARLAEAA RSGKAQRQEL SGSTITLSSL GVLGGIVSTP
VINHPEVAIV GVNRIVERPM VVGGNIVVRK MMNLSSSFDH RVVDGMDAAA FIQAVRGLLE
HPATLFLE
