ID A0A0N0CWI8_9BACI Unreviewed; 445 AA.
AC A0A0N0CWI8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=ADM90_08075 {ECO:0000313|EMBL:KOY83225.1};
OS Lysinibacillus macroides.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=33935 {ECO:0000313|EMBL:KOY83225.1, ECO:0000313|Proteomes:UP000037977};
RN [1] {ECO:0000313|EMBL:KOY83225.1, ECO:0000313|Proteomes:UP000037977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 54 {ECO:0000313|EMBL:KOY83225.1,
RC ECO:0000313|Proteomes:UP000037977};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) 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:KOY83225.1}.
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DR EMBL; LGCI01000005; KOY83225.1; -; Genomic_DNA.
DR RefSeq; WP_053994466.1; NZ_LGCI01000005.1.
DR AlphaFoldDB; A0A0N0CWI8; -.
DR STRING; 33935.ADM90_08075; -.
DR PATRIC; fig|33935.3.peg.1071; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000037977; 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 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 131..168
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 105..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 48214 MW; 8F0EF6E9236B32EB CRC64;
MAVQNITMPQ LGESVTEGTI EKWLVKPGDT VKKYDPLAEV VTDKVNAEIP SSFEGVITEL
IAQEGQTLPV GAVVCSIEIA GDNDLPSPPP EKKSTVSTAI LNAGIQRKQE VQSPASPPPA
APREERKDKI RYSPAVLRLA QEHDIALEHV TGTGEGGRIT RKDLLKLIDS GNIPTAREAA
STPAAAQPPA EPASPVRETQ QQPAAPAQSV QVGDVEIPVT KVRRAIANNM VKSVHEVPHA
WMMMEVDVTD LVAYRDSLKH EFKHKEGFNL TYFAFFVKAV AQALKEFPIM NSTWAEDKII
QKHAINISIA VATDDALFVP VIKHADEKSI KGIAKEIHEL AVKVRAGKLT MDDIKGGTFT
VNNTGAFGSV QSMGIINYPQ AAILQVESIV KKPVVLPGGM FAARDIVNLC LSLDHRVLDG
LVCGKFLNRV KEILENTNKS LTSVY
//
