ID A0A0U4C359_9DEIO Unreviewed; 501 AA.
AC A0A0U4C359;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AUC44_15865 {ECO:0000313|EMBL:ALW90183.1};
OS Deinococcus actinosclerus.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1768108 {ECO:0000313|EMBL:ALW90183.1};
RN [1] {ECO:0000313|EMBL:ALW90183.1, ECO:0000313|Proteomes:UP000060071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BM2 {ECO:0000313|EMBL:ALW90183.1,
RC ECO:0000313|Proteomes:UP000060071};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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}.
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DR EMBL; CP013910; ALW90183.1; -; Genomic_DNA.
DR RefSeq; WP_062159575.1; NZ_CP013910.1.
DR AlphaFoldDB; A0A0U4C359; -.
DR KEGG; dab:AUC44_15865; -.
DR Proteomes; UP000060071; 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: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..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 173..210
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 214..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 53285 MW; 9E40849ABF04470F CRC64;
MKEVLLPELA ESVVEGEILK WLVQEGDTIA LEQPLCEVMT DKVTVELPSP VAGVLSKRLA
GEGDVVAVHA AIALIDETGG AGTVPATQAI QDNAANPGAA EPQLPAQAQE EREQIGGSIV
EAGHLQKGAD DDSTSLFKAF SSDEKVQVQG LGARQPVAPA APTQPTRADG RVLAVPAARQ
LARELNLDLT QVRGSGPNGR IRVSDVLAHQ GINQGQAAPM QTAPAQTAAP AQAPAQAAQP
APAAKAPAAG GMPVAPVQYR TPKGYEHLED RVPLRGMRRA ISNQMQASHL YTVRTLTVDE
VNLSKLVEFR ARVKDDAAAA GVKLSYLPFI FKAVAVALRK FPSLNTSFDE ATQEIVQKRY
YNIGMAVATD AGLTVPVLKD VNHKSVFDLA REVSDLAVRA QGGKLQADEL AGSTFSVTNI
GSIGALFSFP IINVPDAAIL GIHSIQKRPI VDEYDNIVVA HMMYLSLSFD HRLVDGAEAA
RFCKEVIRLL ENPDRLMLEA M
//
