ID A0A1I2EZK9_9ACTN Unreviewed; 602 AA.
AC A0A1I2EZK9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05216251_10751 {ECO:0000313|EMBL:SFE97876.1};
OS Actinacidiphila alni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=380248 {ECO:0000313|EMBL:SFE97876.1, ECO:0000313|Proteomes:UP000199323};
RN [1] {ECO:0000313|EMBL:SFE97876.1, ECO:0000313|Proteomes:UP000199323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFE97876.1,
RC ECO:0000313|Proteomes:UP000199323};
RA de Groot N.N.;
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}.
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DR EMBL; FONG01000007; SFE97876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2EZK9; -.
DR STRING; 380248.SAMN05216251_10751; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000199323; 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; 2.
DR Gene3D; 2.40.50.100; -; 2.
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; IPR014276; 2-oxoglutarate_DH_E2.
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 NCBIfam; TIGR02927; SucB_Actino; 1.
DR PANTHER; PTHR43416:SF8; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000199323};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 136..211
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 299..336
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 60323 MW; 0DF533D8712EA5BD CRC64;
MAVSVTLPAL GESVTEGTVT RWLKAEGERV EADEPLLEVS TDKVDTEIPS PASGVLASIK
VAEDETVEVG AELAVIDDGS GAPAPAAAEQ APAPAAEPTP APAAPEPAAA APSTEQAAPA
PAPTAQAATG GSGASGTDVV LPALGESVTE GTVTRWLKAV GESVEADEPL LEVSTDKVDT
EIPSPVAGTL LEILVQEDET AEVGAKLAVV GAAGAAPAAA PAPAAPAPAA APEPAAPAPA
PAAPAPAPQA PTAPAPQQQT APAPDPAPSQ PAPAPAPAPA PVAPAAPAPA ATSGDDGAYV
TPLVRKLASE SGVDLGSVRG TGVGGRIRKQ DVLAAAEAAK AAAPAPQATA STAKKAPALE
ASPLRGQTVK MPRIRKVIGD NMVKALHEQA QLSSVVEVDV TRIMRLRGLA KESFAAREGV
KLSPMPFFVK AAAQALKAHP AINARINVDE GTITYFDTES IGIAVDSEKG LMTPVIKHAG
DLNVAGIAKA TADLAGKVRS NKITPDELSG ATFTISNTGS RGALFDTIIV PPNQVAILGI
GATVKRPAVI ETEEGTVIGV RDMTYLTLSY DHRLVDGADA ARYLTAVKEI LEAGEFEVEL
GL
//
