ID A0A0M9DTL4_9BACT Unreviewed; 447 AA.
AC A0A0M9DTL4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AD998_12030 {ECO:0000313|EMBL:KOY86772.1};
OS bacterium 336/3.
OC Bacteria.
OX NCBI_TaxID=1664068 {ECO:0000313|EMBL:KOY86772.1, ECO:0000313|Proteomes:UP000037950};
RN [1] {ECO:0000313|EMBL:KOY86772.1, ECO:0000313|Proteomes:UP000037950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=336/3 {ECO:0000313|EMBL:KOY86772.1,
RC ECO:0000313|Proteomes:UP000037950};
RA Isojarvi J., Battchikova N., Aro E.-M.;
RT "Draft genome sequence of symbiotic bacteroides-like organism.";
RL Submitted (JUL-2015) 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:KOY86772.1}.
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DR EMBL; LJIE01000001; KOY86772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9DTL4; -.
DR STRING; 1664068.AD998_12030; -.
DR PATRIC; fig|1664068.3.peg.2448; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000037950; 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|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000037950};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 119..159
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 447 AA; 49101 MW; 4EC1F63F7D4BC7D8 CRC64;
MALVELVMPK MGESVMEGTI LNWLKKVGDK IEQDESILEV ATDKVDTEIP STHAGVLKEV
LVKEGDVVQV GKTIAVIDTG GGASQPQTTP TQEVVKEAQK IEAKIEEVKT LSEPIAGRFY
SPLVLNIAKE EGISMSELET IAGTGQEGRV TKNDILAYVK AKQSGGTVIQ QPKTVEPVIE
VKPVEEIQVT PVQEVKVVQP EKKSTPVPIF AGDEVIEMDR MRKMIAQRMV ESKHTAPHVT
SFVEADVTNL VYWRRKVKDE MLQKEGEALT FMPMFIEAIS KALKDYPMMN ISVDGDKIIK
RKNINIGMAV ALPSGNLIVP VIQNTDQLNL VGLTKKINDI ARRARENKLK PDELVGGTYT
VSNVGSFGNV LGTPIIMQPQ VGILALGAIR KQASVIETPF GDTIGVRHMM YLSHSYDHRV
VDGALGGMFV RRVADYLEEF DLSKSLF
//
