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
//