ID A0A0H5CRV7_9PSEU Unreviewed; 457 AA.
AC A0A0H5CRV7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
OS Alloactinosynnema sp. L-07.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK60589.1, ECO:0000313|Proteomes:UP000076116};
RN [1] {ECO:0000313|Proteomes:UP000076116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-07 {ECO:0000313|Proteomes:UP000076116};
RA Ramaraj T.;
RL Submitted (MAY-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; LN850107; CRK60589.1; -; Genomic_DNA.
DR RefSeq; WP_054053109.1; NZ_LN850107.1.
DR AlphaFoldDB; A0A0H5CRV7; -.
DR STRING; 1653480.gene:80949475; -.
DR KEGG; alo:CRK60589; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000076116; Chromosome i.
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 ECO:0000313|EMBL:CRK60589.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:CRK60589.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076116};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:CRK60589.1}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 175..212
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 457 AA; 47949 MW; 8C8EAFD050E8150E CRC64;
MPEYKTFPLP DTAEGLTEAE ILSWHVKPGD TVTVNQIIVE IETAKAAVEL PCPWAGVVTE
LHVKPGQTVD VGAPILTIDV DPGGAAKPTN GSTPAAAAPV EEEMKPLVGY GSKTVTAKRR
ARKGPAVPAS AAAEAAQSTV AAAFEHHQGP VPDPEPVVPD SPAALLDLPG GYVPLAKPPV
RKLAKDLGVD IRSLTGSGES GVITRADVER AASGPVDTPA AVVAPRGERR VPIKGVRKVT
AQAMVASAFT APHVTEFLTL DVTPMMELRA KLKNHPEFRG VKLTPLAFCA KAIAMAVRRT
PEVNSSWDEA AQEIVYKDYV HLGIAAATPR GLIVPKIRDA DTLSLRELAE ALDLLTTTAR
DGKTPPADMV NGTITITNVG VFGVDTGTPI INPGESAILA FGAIRDTPWV VDGEIKIRKV
CQLALSFDHR LVDGQQGSEF LADVGALLAD PALAITY
//
