ID A0A1X2D7Y0_9MYCO Unreviewed; 400 AA.
AC A0A1X2D7Y0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AWC22_13540 {ECO:0000313|EMBL:ORW84262.1};
OS Mycobacterium riyadhense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=486698 {ECO:0000313|EMBL:ORW84262.1, ECO:0000313|Proteomes:UP000193087};
RN [1] {ECO:0000313|EMBL:ORW84262.1, ECO:0000313|Proteomes:UP000193087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45176 {ECO:0000313|EMBL:ORW84262.1,
RC ECO:0000313|Proteomes:UP000193087};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-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}.
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:ORW84262.1}.
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DR EMBL; LQPQ01000037; ORW84262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2D7Y0; -.
DR STRING; 486698.AWC22_13540; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000193087; 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; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 7..85
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 129..167
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 400 AA; 42357 MW; ACA6F537F14F7416 CRC64;
MNADDRVKSF RVPDLGEGLE DVTVTSWEVA VGDDVELNQT LCTVETAKAE VEIPSPYSGR
IVEIGGSTGD VGDVIKVGAM LVRIDTEPLN GDVKRQMPSG TNGEADVPTL VGYGADSSID
TSRRPSRPLA APPARKLAKE LTVDLTSLPQ GSGAGGVITR ADVLAAAHVE AADVRPVHGV
QTRMAEKMAL SHKEIPAAKA SVEVACTELQ RLSDRFRSVA PEITPFVLTL RLLVIALTHN
EILNSTWVES PEGPQVHVHR GVHLGFGVAT KRGLLVPVIT DAHNKTTREL ASRTAELITG
AREGTLTPAE LRGSTFTVSN FGALGVDDGV PVINHPEAAI LGMGAIKPRP VAVGDEVVVR
PTMTLTCVFD HRVADGAQVA QFVCELRDLI ESPESALLDL
//
