ID   A0A2T4U4N8_9BACI        Unreviewed;       429 AA.
AC   A0A2T4U4N8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=C6Y45_11440 {ECO:0000313|EMBL:PTL38367.1};
OS   Alkalicoccus saliphilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX   NCBI_TaxID=200989 {ECO:0000313|EMBL:PTL38367.1, ECO:0000313|Proteomes:UP000240509};
RN   [1] {ECO:0000313|EMBL:PTL38367.1, ECO:0000313|Proteomes:UP000240509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6AG {ECO:0000313|EMBL:PTL38367.1,
RC   ECO:0000313|Proteomes:UP000240509};
RA   Zhao B.;
RT   "Alkalicoccus saliphilus sp. nov., isolated from a mineral pool.";
RL   Submitted (MAR-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:PTL38367.1}.
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DR   EMBL; PZJJ01000019; PTL38367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4U4N8; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000240509; 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; 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; 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; 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};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          105..142
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   DOMAIN          152..189
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          86..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  47429 MW;  D0B50B068B0FC164 CRC64;
     MASEVLMPKL GAQMEEGTIV SWLVELGEFI EKGDPLVEIQ TDKVTMEVEA EHEGHLIKII
     FEENEAVPVH TPIAYIGEKG EKVKAKVEGS QNKEEEKQQS NVKTPRTPLA RKIAEEENIS
     LDQVTGTGPN GRIQKKDILI YQSEKEAKPA KRATPLAKKV AEKQNIDINE VEGSGHYGKV
     NKEDVLTLSS NSPADTSQER SEMVKPIKGL RRAIAESMKK SAFEAPHVTL YSEIDMTEAV
     QLRNMLLPLI EEKEKVRISF NDIILKAVGD TLHKHPGMNI SFNKDQITYH EKVNIGMAVA
     IEDGLVVPVI RNITNKTLSD ITKETKDLGR RAIVHQLKGE EMKGSTFTVS NLGKYAVDHF
     NPIINQPNAA ILGIGQISKK PAVKQGEVTV RSIMGVSLSF DHRALDGAPA AAFLSDVKRL
     LEDPFKLLI
//