ID W4APG2_9BACL Unreviewed; 481 AA.
AC W4APG2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=C161_20292 {ECO:0000313|EMBL:ETT33395.1};
OS Paenibacillus sp. FSL R5-192.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT33395.1, ECO:0000313|Proteomes:UP000019041};
RN [1] {ECO:0000313|EMBL:ETT33395.1, ECO:0000313|Proteomes:UP000019041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT33395.1,
RC ECO:0000313|Proteomes:UP000019041};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETT33395.1}.
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DR EMBL; ASPR01000042; ETT33395.1; -; Genomic_DNA.
DR RefSeq; WP_036672332.1; NZ_ASPR01000042.1.
DR AlphaFoldDB; W4APG2; -.
DR PATRIC; fig|1226754.4.peg.4114; -.
DR Proteomes; UP000019041; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
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; 1.
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; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ETT33395.1}.
FT DOMAIN 7..82
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 130..167
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 96..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 52097 MW; 4F76D1C7A1972376 CRC64;
MAERMKWIEV IMPQLAESLV SATIGKWLKK PGDRVEQYEP ICEVITDKVN AEIPSTVDGI
MGDLLVEEGT TIAVGEAICR MQVAASDEEA AEQVTQVSQQ QEQVQQHASP TPLAASNTAG
HDPNQPMRNR YSPAVQSLAA EHGLNLQSIQ GTGAGGRITR KDVLTFVAQG GNAAGSSAQA
SSAAVQHTPS SMPSASPFSG VNRGNGEMGL TAGEAISASD AGVPVRHSGI HLTESPKIPQ
IEVEGGGQGR SEYFIDVTPV RNAIARNMRQ SVSEIPHAWT MIEVDVTNLV MLRNKLKDEF
KRKEGINLTY LSFMMKGVVN AIKDYPIMNS VWAVDKIIVK RDINLSMAVG TEDSVLTPVI
KHADQRNIAG LAREVDELAR KTREGTLKLD HMQGGTFTVN NTGSFGSILS QPIINYPQAA
ILTFESIVKK PVVINDMIAV RSMANLCLSL DHRILDGVIS GRFLQRVKEN LEGYTMETKV
Y
//
