ID A0A0J6WXF0_9FIRM Unreviewed; 440 AA.
AC A0A0J6WXF0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, 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=AB840_03635 {ECO:0000313|EMBL:KMO87304.1};
OS Megasphaera cerevisiae DSM 20462.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1122219 {ECO:0000313|EMBL:KMO87304.1, ECO:0000313|Proteomes:UP000036503};
RN [1] {ECO:0000313|EMBL:KMO87304.1, ECO:0000313|Proteomes:UP000036503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20462 {ECO:0000313|EMBL:KMO87304.1,
RC ECO:0000313|Proteomes:UP000036503};
RA Kutumbaka K., Pasmowitz J., Mategko J., Reyes D., Friedrich A., Han S.,
RA Martens-Habbena W., Neal-McKinney J., Janagama H.K., Nadala C.,
RA Samadpour M.;
RT "Draft genome sequence of beer spoilage bacterium Megasphaera cerevisiae
RT type strain 20462.";
RL Submitted (JUN-2015) 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}.
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:KMO87304.1}.
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DR EMBL; LEKT01000007; KMO87304.1; -; Genomic_DNA.
DR RefSeq; WP_048513462.1; NZ_LEKT01000007.1.
DR AlphaFoldDB; A0A0J6WXF0; -.
DR STRING; 39029.BSR42_01725; -.
DR PATRIC; fig|1122219.3.peg.2824; -.
DR InParanoid; A0A0J6WXF0; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000036503; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
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; 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; 2.
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:UP000036503};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 119..156
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT DOMAIN 162..196
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 440 AA; 46385 MW; 885561A6FC04EBD5 CRC64;
MAAEITMPQL GLTMTEGTVS QWLKHEGDIV KKGDELVEIE TDKISNIVEA HEDGVLLKIV
AQEGESLPVK ALLGYIGQPG EQIGAAASAA AVPDSAKSMA APALREAPVQ KIAAGGWVPA
TPYARKLARD GGLDLTLVTG TGYNGRVIGS DVADCKTAAT VRISPTAAKV AADLGIDPAA
IQTAGRIMKA DVLQSAGIAA AAVAAVPQVT ASPVSVVPAH GEKLKGMRKV IAQRLGEGWR
NTPHVHHTVE INMTEAAALR GKFIAMDRKF SFTDLIIKAM CKVLEEYRNA NDSLDGAYII
HNPEINMGVA VAIDGGLIVP VIKNANQLGL MDIHQKVGEL ARKAREHTLS PDELSGGTCT
ISNLGMYGCD HFTPIVNPPE AAILGVCRTV EKAVVIDHQI VIAPMMNAVL GYDHRIIDGA
TAGLVTSRLR EYLENPLLLL
//
