ID A0A1X0GN70_9MYCO Unreviewed; 585 AA.
AC A0A1X0GN70;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, 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};
GN ORFNames=BST36_27200 {ECO:0000313|EMBL:ORB15481.1};
OS Mycolicibacterium moriokaense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=39691 {ECO:0000313|EMBL:ORB15481.1, ECO:0000313|Proteomes:UP000192354};
RN [1] {ECO:0000313|EMBL:ORB15481.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP105393 {ECO:0000313|EMBL:ORB15481.1};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-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 -!- 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:ORB15481.1}.
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DR EMBL; MVIB01000039; ORB15481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0GN70; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000192354; 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 Pyruvate {ECO:0000313|EMBL:ORB15481.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ORB15481.1}.
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 275..312
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 77..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 61032 MW; 89B63842E686996A CRC64;
MAISVQMPAL GESVTEGTVT RWLKQEGDTV EQDEPLLEVS TDKVDTEIPS PAAGVLQKIV
AQEDDTVEVG GELAIIGEAG ESSGGDSGAD EAPAEEPAEE EKPAEEPAAQ EAPAAEEQEA
APEPAPKPAA ASSGSTTPVL MPELGESVTE GTVTRWLKKV GDSVEVDEPL VEVSTDKVDT
EIPSPVAGTL VSITAEEDDT VAVGGELAKI GDAGAAAEAA PEPEPEPKPE PKPEPVQEAK
PEPKPDPKPE PKPEPKPEPK PAPAAEAPSG DGSPYVTPLV RKLAAENDID LATVKGTGVG
GRIRKQDVLA AAEAKKAPAA APAAQAPSSA PAPKEAPAPA PALAHLRGTT QKANRIRQLT
AKKTRESLQA TAQLTQTHEV DMTKIVALRA RAKNEFAERE GVNLTYLPFI ARAVIDALKA
HPNINASYNE ETKEITYYDA EHLGFAVDTE QGLLSPVIHN AGDLSLGGLA RAIADIAARA
RSGNLKPDEL SGGTFTITNI GSQGALFDTP ILVPPQAAML GTGAIVKRPR VIVDDFGNES
IGVRSICYLP LTYDHRLIDG ADAGRFLTTV KRRLEEGAFE ADLGL
//
