ID A0A1S2MWQ0_9MICO Unreviewed; 459 AA.
AC A0A1S2MWQ0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BK819_07560 {ECO:0000313|EMBL:OIJ33628.1};
OS Microbacterium sp. LCT-H2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1914306 {ECO:0000313|EMBL:OIJ33628.1, ECO:0000313|Proteomes:UP000179624};
RN [1] {ECO:0000313|EMBL:OIJ33628.1, ECO:0000313|Proteomes:UP000179624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCT-H2 {ECO:0000313|EMBL:OIJ33628.1,
RC ECO:0000313|Proteomes:UP000179624};
RA Huang B.;
RT "Draft genome sequence of strain LCT isolated from the Shenzhou X
RT spacecraft of China.";
RL Submitted (OCT-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:OIJ33628.1}.
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DR EMBL; MODW01000002; OIJ33628.1; -; Genomic_DNA.
DR RefSeq; WP_071328579.1; NZ_MODW01000002.1.
DR AlphaFoldDB; A0A1S2MWQ0; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000179624; 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; 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 SUPFAM; SSF52777; CoA-dependent acyltransferases; 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:OIJ33628.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:OIJ33628.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 158..195
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 77..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 48336 MW; 318AE7EBBA9F23B4 CRC64;
MIAEFRLPDL GEGLTEAEVV HWLVAPGDSV TLNQTLAEVE TAKAVVELPS PYEGTVSTLH
ADAGETVAVG APLIAFDIEG EDPPPTPSGG EQEASPEKAQ PNLVGYGAAP TSSGRPARRA
RRRSAAQVAS AADTAVLEAA PHDATPSVAV EPILERPRST PPVRAYAKRR GVDLVLVAAE
IGDRVITRAD VDAYAERIGA DPSRPARAPE RVTTAASGTL PPAEGRPRET RIPIRGVRKH
TAAAMVQSAF TAPHVTVFHT VDVTATMEML ARLRDDRALA AHRIGPLAVV AKAVCLALRR
APGLNARWDE ESGEIVEYGF VDLGIAAATE RGLIVPMIRD AERMNLVELS AAIRALAETA
RAGKTSPAEL AGGTFSLSNI GVFGVDAGTP ILPPGQSGIL AVGAVRRQPW EYRGEIALRQ
LMTLSLSFDH RLVDGAEGAT FLKDVADILE DPGRAMLLS
//
