ID M5P4W4_9BACI Unreviewed; 441 AA.
AC M5P4W4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=BSONL12_11736 {ECO:0000313|EMBL:EME74459.1};
OS Bacillus sonorensis L12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1274524 {ECO:0000313|EMBL:EME74459.1, ECO:0000313|Proteomes:UP000011907};
RN [1] {ECO:0000313|EMBL:EME74459.1, ECO:0000313|Proteomes:UP000011907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12 {ECO:0000313|EMBL:EME74459.1,
RC ECO:0000313|Proteomes:UP000011907};
RX PubMed=23538904;
RA Adimpong D.B., Sorensen K.I., Nielsen D.S., Thorsen L., Rasmussen T.B.,
RA Derkx P.M., Jespersen L.;
RT "Draft Whole-Genome Sequence of Bacillus sonorensis Strain L12, a Source of
RT Nonribosomal Lipopeptides.";
RL Genome Announc. 1:E0009713-E0009713(2013).
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:EME74459.1}.
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DR EMBL; AOFM01000007; EME74459.1; -; Genomic_DNA.
DR RefSeq; WP_006638334.1; NZ_AOFM01000007.1.
DR AlphaFoldDB; M5P4W4; -.
DR STRING; 1274524.BSONL12_11736; -.
DR GeneID; 79845930; -.
DR PATRIC; fig|1274524.3.peg.2533; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000011907; 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}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 139..176
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 85..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 47504 MW; 56083EB2F8B515D5 CRC64;
MAFEFKLPDI GEGIHEGEIV KWFVKPNDEV NEDDVLAEVQ NDKAVVEIPS PVKGKVLELK
VEEGTVATVG QTIITFDAPG YEDLQFKGDS GDAKTEEQVQ SSAEGGQDLD KKERPEEPVQ
ETGAGKQDQA DADPNKRVIA MPSVRKYARE KGVEITKVAG SGKNGRVLKE DIDSFLSGGN
AEAQAAPADQ KAEPAAQPAA AAQAPEGEFP ETREKMSGIR KAIAKAMVNS KHTAPHVTLM
DEVDVTNLVA HRKQFKQVAA DQGIKLTYLP YVVKALTSAL KKYPVLNTSI DDSTDEVIQK
HYFNIGIAAD TEKGLLVPVV KHADRKAIFE ISNEINELAS KAREGKLAPA EMKGASCTIT
NIGSAGGQWF TPVINHPEVA ILGIGRIAEK AVVRDGEIVA APVLALSLSF DHRMIDGATA
QNALNHIKRL LNDPQLILME A
//
