ID E0RAQ1_PAEP6 Unreviewed; 537 AA.
AC E0RAQ1;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN OrderedLocusNames=PPE_02530 {ECO:0000313|EMBL:ADM70360.1};
OS Paenibacillus polymyxa (strain E681).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=349520 {ECO:0000313|EMBL:ADM70360.1, ECO:0000313|Proteomes:UP000002227};
RN [1] {ECO:0000313|EMBL:ADM70360.1, ECO:0000313|Proteomes:UP000002227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E681 {ECO:0000313|EMBL:ADM70360.1,
RC ECO:0000313|Proteomes:UP000002227};
RX PubMed=20851896; DOI=10.1128/JB.00983-10;
RA Kim J.F., Jeong H., Park S.Y., Kim S.B., Park Y.K., Choi S.K., Ryu C.M.,
RA Hur C.G., Ghim S.Y., Oh T.K., Kim J.J., Park C.S., Park S.H.;
RT "Genome sequence of the polymyxin-producing plant-probiotic rhizobacterium
RT Paenibacillus polymyxa E681.";
RL J. Bacteriol. 192:6103-6104(2010).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; CP000154; ADM70360.1; -; Genomic_DNA.
DR RefSeq; WP_013310509.1; NC_014483.2.
DR AlphaFoldDB; E0RAQ1; -.
DR KEGG; ppy:PPE_02530; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_9; -.
DR OMA; HPCIMAP; -.
DR Proteomes; UP000002227; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 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 PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423}; Hydrolase {ECO:0000313|EMBL:ADM70360.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
SQ SEQUENCE 537 AA; 57130 MW; DBBE826A13AC302B CRC64;
MAKFEYKFPE LGEGLHEGEI IKMHIKPGDK VTDEDIIMEV QNDKAVVEVP CPVNGTVQEV
FAKDGDIFNV GQVVAVIDAE GELPEQEDAP EAPAASPEPS AAAQGGAAGA ARFEYKFPEL
GEGLHEGEII KMHIKPGDKV TDEDIIMEVQ NDKAVVEVPC PVNGTVQEVF AKDGDIFNVG
QVVAVIAAEG ELPEQEEAPA AAKQEQDAAQ GGANTKPAAT PAASNKDVLA TPSVRKFARE
QGVNIAQVNG SGKNGKITKE DVEAFKNGGG QAAAPVAKEA AKAQEPAKKE AKAAASSAPA
ADPRAEEERV PFKGIRKAIS NAMVKSAYTA PHVTIMDEVD VTELVAFRTR IKPIAEKKGT
KVTYLPFIVK ALVAASRQFP ALNATIDEEA NEIVYKKYYN IGIATDTDNG LIVPVIKDAD
RKSIWMIADS IRDLAVRGRD GKLAANEMRG STISITNIGS AGGMFFTPII NFPEVAILGT
GRISEKAVVK NGEIVAAPVM ALSLSFDHRI IDGATAQNFM NYIKQLLANP ELLVMEV
//