ID A0A0M8YTM0_9ACTN Unreviewed; 469 AA.
AC A0A0M8YTM0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ADL06_00030 {ECO:0000313|EMBL:KOX38625.1};
OS Streptomyces sp. NRRL F-6491.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX38625.1, ECO:0000313|Proteomes:UP000037743};
RN [1] {ECO:0000313|EMBL:KOX38625.1, ECO:0000313|Proteomes:UP000037743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX38625.1,
RC ECO:0000313|Proteomes:UP000037743};
RA Noorani M.;
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:KOX38625.1}.
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DR EMBL; LGEE01000001; KOX38625.1; -; Genomic_DNA.
DR RefSeq; WP_053640114.1; NZ_LGEE01000001.1.
DR AlphaFoldDB; A0A0M8YTM0; -.
DR PATRIC; fig|1519495.3.peg.6; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000037743; 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|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 1..71
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 165..202
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 116..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 48184 MW; 817B58BB5D12FEA8 CRC64;
MPDVGEGLTE AEILKWYVQP GDTVTDGQVV CEVETAKAAV ELPIPFDGTV HELCFPEGTT
VDVGQVIISV NVGGGAPPAP AAPVTESVAA QAVPAEPVAE EDEPQGRQPV LVGYGVAASS
TKRRPRKAAG SGEAAPAAAP AQPAPVAVSV PEQLNGHASG AGRPLAKPPV RKLAKDLGVD
LATVVPSGPD GIITREDVHA AAVPAPAPAA EAPAPVRAPA PVPAAAPAAA PAAEAGARET
RVPIKGVRKA TAAAMVGSAF TAPHVTEFVT FDITRTMKLV EELKSDKDMA GLRVNPLLLI
AKAILVAVRR NPEINAAWDE AAQEIVLKHY VNLGIAAATP RGLIVPNIKD AHAQTLPELS
KSLSELVATA REGKTTPAAM QGGTFTITNV GVFGVDTGTP ILNPGESAIL AVGAIKLQPW
VHKGKVKPRQ VTTLALSFDH RLVDGELGSK FLADVAAILE QPKRLITWA
//
