ID A0A290XAE6_9GAMM Unreviewed; 483 AA.
AC A0A290XAE6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=CNR27_00030 {ECO:0000313|EMBL:ATD66043.1};
OS Luteimonas chenhongjianii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=2006110 {ECO:0000313|EMBL:ATD66043.1, ECO:0000313|Proteomes:UP000218968};
RN [1] {ECO:0000313|Proteomes:UP000218968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=100111 {ECO:0000313|Proteomes:UP000218968};
RA Gui Z.;
RT "Luteimonas liuhanmingii sp.nov., isolated from the intestinal contents of
RT Tibetan Plateau Pika in Yushu, Qinghai Province, China.";
RL Submitted (SEP-2017) 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 -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; CP023406; ATD66043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A290XAE6; -.
DR KEGG; lum:CNR27_00030; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000218968; Chromosome.
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:SF12; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 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 Reference proteome {ECO:0000313|Proteomes:UP000218968};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 174..211
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 86..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 49935 MW; DC95B6E5E0979CBC CRC64;
MANPTSFRLP DLGEGLPDAT IVEWAVKVGD TIRLDDALVS METAKAVVDV PSPVSGRVLR
LAGEPGDIIE TGAILAEFEI DISQPQRAEG QDTGHHHGPP KSTPGKGVGS QDPAPDDKVV
ASSEGGAISA SDEAQPEAKS EAAGGRADSG TVVGAMQSSD AVRSEQASSA GGVKAMPAVR
ALARKLKVDI VRVRPSGADG VVTMADVKQA AADGSAAQGA PGPRSGELES AASHARPAPA
PAAQPVRQAS ERTALSASGK PMRTQPPTVS ASGQPEPLKG VRRNMARVMA DAHAKVVPTT
LSDDADIHAW TPGNDVTSRL IRAICVAARA VPALNAWFDG DKLTRTLHPH VDIGIAVDTD
DGLFVPALRN ADMLDARGVR EGINRLRAQV EDRSIPGSEL TGYTISLSNF GMFAGRYATP
VVVPPCVAIV AAGRGRHQIT PVIGGFESHK VIPLSLTFDH RAATGGEAAR FLKAMLDDLA
LPN
//
