ID A0A0X8KMT1_9BACL Unreviewed; 463 AA.
AC A0A0X8KMT1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AXE85_07640 {ECO:0000313|EMBL:AME10025.1};
OS Gemella sp. oral taxon 928.
OC Bacteria; Bacillota; Bacilli; Bacillales; Gemellaceae; Gemella.
OX NCBI_TaxID=1785995 {ECO:0000313|EMBL:AME10025.1, ECO:0000313|Proteomes:UP000063069};
RN [1] {ECO:0000313|Proteomes:UP000063069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W2231 {ECO:0000313|Proteomes:UP000063069};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00043782};
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; CP014233; AME10025.1; -; Genomic_DNA.
DR RefSeq; WP_062174447.1; NZ_CP014233.1.
DR AlphaFoldDB; A0A0X8KMT1; -.
DR STRING; 1785995.AXE85_07640; -.
DR KEGG; got:AXE85_07640; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000063069; Chromosome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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; 2.
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; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 2.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423}; ATP-binding {ECO:0000313|EMBL:AME10025.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Nucleotide-binding {ECO:0000313|EMBL:AME10025.1};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 120..157
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT DOMAIN 163..200
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 463 AA; 49789 MW; CA294C3399604578 CRC64;
MAVEVIMPKA GSEMEEGEIV QWFKKEGDHV EAGEVLLEIV TDKVNMEVEA DASGTLLKIL
AQAGDVVPVV QTIAWIGEKG EEIPGASATG EVAPAETIVE KKVDVTPVKE IEKIDYSGLR
ATPAARAYAR EKGIDLAKVK GTGAKGRIHK EDVLEYKLNS KVKISPLAER IAEIEGVSTT
GIVGTGPNGK IMKADVLAVL HGTPKAAPVK KEEVAPAKAK KAPLAPNENQ WGVVETVPMS
PMRKVISKRM SESYFSAPTF VVNVEVDMTE LLALRKKVVD TIIEETGKKA TVTDFISLAV
IKSLMKHPYV NASLSKDEKE MYLHHYVNLS IAVGMDSGLV VPVIKGADKM SLKELVVASK
EITTKALNGK LKPDEMADST FTISNLGMYG VKSFVPIINQ PNTAILGVSA TVPKPVVMNG
EIVVRPIMTL TLTADHRVVD GLEGAKFMKT LKEAIENPLS LLI
//
