ID A0A1P8Q5A3_9LACO Unreviewed; 424 AA.
AC A0A1P8Q5A3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BTM29_10905 {ECO:0000313|EMBL:APX73026.1};
OS Companilactobacillus allii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1847728 {ECO:0000313|EMBL:APX73026.1, ECO:0000313|Proteomes:UP000187499};
RN [1] {ECO:0000313|Proteomes:UP000187499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WiKim39 {ECO:0000313|Proteomes:UP000187499};
RA Jung M.Y., Lee S.H.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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; CP019323; APX73026.1; -; Genomic_DNA.
DR RefSeq; WP_076617545.1; NZ_RHNV01000006.1.
DR AlphaFoldDB; A0A1P8Q5A3; -.
DR STRING; 1847728.BTM29_10905; -.
DR KEGG; lalw:BTM29_10905; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000187499; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000187499};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 123..160
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 71..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 45732 MW; 20A77647679A0350 CRC64;
MAYKFKLPEL GEGMAEGEIA SWLVKEGDTI KEDDSIVEIQ NDKSVEELPS PVSGTVKQIV
AQEGDTVEIG DTLIVIDDGS ADTGDDEEAP KADKAPEKAD APADKSAEKA PSQATGSAND
NYLAMPSVRQ YARDEGVDLS LVTPSGKHGQ ISKEDIDSYK AGAPAKASKT EETPAKASGP
AVKPYKSDEP ELETREKMSM TRKAIAKAMR NSKDIAPHVT SFDDVEVSVL MANRKKYKSV
AADKGIKLTF LPYIVKALVA VMKEYPEFNA SIDNSTDEIV YKHYYNVGIA TNTEHGLYVP
NIKNADSKGM FEIAKEITEN TQAAYDNKLN SKAMSGGSIT ISNVGSIGGG WFTPVINQPE
VAILGVGKIA NEPYVDEDGN IQVGKMLKLS LSYDHRLIDG ALAQNALNLL KKLLHEPDML
LMEG
//
