ID A0A1I1QSL9_9BURK Unreviewed; 447 AA.
AC A0A1I1QSL9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05216204_1204 {ECO:0000313|EMBL:SFD25035.1};
OS Massilia yuzhufengensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1164594 {ECO:0000313|EMBL:SFD25035.1, ECO:0000313|Proteomes:UP000198639};
RN [1] {ECO:0000313|EMBL:SFD25035.1, ECO:0000313|Proteomes:UP000198639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12041 {ECO:0000313|EMBL:SFD25035.1,
RC ECO:0000313|Proteomes:UP000198639};
RA de Groot N.N.;
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 -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; FOLD01000020; SFD25035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1QSL9; -.
DR STRING; 1164594.SAMN05216204_1204; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000198639; 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 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 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 159..196
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 84..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 47760 MW; 823E38192399419D CRC64;
MGIHVIKMPD LGEGIAEVEV VAWHVQPGDT VKEDQVLADV MTDKATVEIP SPVAGTITSL
GGAIGQSMAV GAELIRLEVE GAGNYSGDKA KQEPVKSAAA TAPAEEVGEP QLEAVAAAEA
SSHATARAPA PAAPRPAQQP PQRGQQAPAP MRADGDKPHA APAVRQRAWD LGIELQFVHG
SGPAGRITHA DLDEHVSGRR QGGARAGSDN RYAQLHGEHA TPIIGLRRKI AEKMQEAKRQ
IPHFTYVEEI DVTELELLRA QLNARYGAER GKLTLLPLLM RAVVLAIRAY PMMNARYDDQ
NNLLTQYEPV HLGIAAQTEA GLMVPVVRHA EARDPWDSAL EVARLADAAR SGKATRDELT
GSTITITSLG PLGGIVTTPV INRPEVAIIG TNRIVDRPVI KDGAMVARKM MNLSSSFDHR
VIDGQVAAKF IQAIRGYLET PATIFVE
//
