ID A0A421BHV4_9LACT Unreviewed; 449 AA.
AC A0A421BHV4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=D3H64_01335 {ECO:0000313|EMBL:RLK63995.1};
OS Atopobacter sp. AH10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Atopobacter.
OX NCBI_TaxID=2315861 {ECO:0000313|EMBL:RLK63995.1, ECO:0000313|Proteomes:UP000283681};
RN [1] {ECO:0000313|EMBL:RLK63995.1, ECO:0000313|Proteomes:UP000283681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH10 {ECO:0000313|EMBL:RLK63995.1,
RC ECO:0000313|Proteomes:UP000283681};
RA Jeong H., Chang D.-H., Kim B.-C.;
RT "Genome sequence of Atopobacter sp. AH10.";
RL Submitted (SEP-2018) 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}.
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:RLK63995.1}.
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DR EMBL; QXPZ01000003; RLK63995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421BHV4; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000283681; 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 Reference proteome {ECO:0000313|Proteomes:UP000283681};
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"
SQ SEQUENCE 449 AA; 48711 MW; 3DD0643D9DBA8346 CRC64;
MAFQFKLPDI GEGIAEGEIV KIDVSVGDTI QEDDTLVEVQ NDKSVEEIPS PVTGKVVKVN
VEEGTVARVG DVIIEIETGD PELDGGVAAA DGTSVEKSSP AREVVEETLD SPISSTSETV
AVEEAQPALD PSDPNKRVLA MPSVRQYARE KGVNIHLVTP SGKNGHVTRE DIDSYASNAS
KVLAPVPEAN KEADLVPSAS VTSRVEKQAY VSLSPELERR EKLSKMRRLI SEAMVNSKHT
APHVTLFDQV EVSKLWEHRK RFKDVALEQG IKLTFLPYVV KALVATVKKF PILNASIDDV
NEEIVYKDYY NIGIATDTPA GLFVPNVKNA NSKSMFAIAD EINHLAQLAH DGKLDRDQMS
NGTITISNIG SARGAFFTPI INYPEVAILG MGTIAQEPVV DEKGNIVVGR VLKLSLSFDH
RIVDGATAQK AMNELKRLLA DPELLLMEG
//