ID A0A1S2LMH5_9BACI Unreviewed; 433 AA.
AC A0A1S2LMH5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=BKP37_12505 {ECO:0000313|EMBL:OIJ13313.1};
OS Anaerobacillus alkalilacustris.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=393763 {ECO:0000313|EMBL:OIJ13313.1, ECO:0000313|Proteomes:UP000179524};
RN [1] {ECO:0000313|EMBL:OIJ13313.1, ECO:0000313|Proteomes:UP000179524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18345 {ECO:0000313|EMBL:OIJ13313.1,
RC ECO:0000313|Proteomes:UP000179524};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-2016) 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:OIJ13313.1}.
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DR EMBL; MLQR01000029; OIJ13313.1; -; Genomic_DNA.
DR RefSeq; WP_071309912.1; NZ_MLQR01000029.1.
DR AlphaFoldDB; A0A1S2LMH5; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000179524; 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|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 125..162
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 83..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 46973 MW; 5A8A1D28AC8CB6BD CRC64;
MAFEFKLPDI GEGIHEGEIV KWFVKPGDEV KEDDILLEVQ NDKAVVEIPS PVEGKILELK
VTEGTVAVVG DVLVTIDYDG EIPASAHGHH DEEEAEVSEP VQEATSTESS QPAVEVEVDE
TRRIISMPSV RKYAREKGID IRKVQGSGNN GRILKADIDN FGNGAPTAAQ APTETETNVE
AQARNAEVKK EVKPYVPVHG ELETREKMSG IRKAISNAMV NSKHTAPHVT LMDEVDVTDL
VAHRSKFKAV AADKGIKLTY LPYVVKALTS ALREYPALNA SIDDVNEEVV YKHYYNIGIA
ADTDKGLLVP VVKDADRKSI FKISSEINEL AIKAREGKLA PDAMKGGSCT ITNIGSAGGQ
WFTPVINHPE VAILGIGRIA EKPVVKNGEI VVAPVLALSL SFDHRLIDGA TAQNALNHIK
RLLNDPQLLV MEA
//
