ID   A0A1R4J8T1_9MICO        Unreviewed;       470 AA.
AC   A0A1R4J8T1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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=FM104_06070 {ECO:0000313|EMBL:SJN28488.1};
OS   Microbacterium esteraromaticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=57043 {ECO:0000313|EMBL:SJN28488.1, ECO:0000313|Proteomes:UP000196320};
RN   [1] {ECO:0000313|EMBL:SJN28488.1, ECO:0000313|Proteomes:UP000196320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B Mb 05.01 {ECO:0000313|EMBL:SJN28488.1,
RC   ECO:0000313|Proteomes:UP000196320};
RA   Peterson S.W.;
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}.
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DR   EMBL; FUKO01000019; SJN28488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4J8T1; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000196320; 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   ECO:0000313|EMBL:SJN28488.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196320};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:SJN28488.1}.
FT   DOMAIN          6..81
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          174..211
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          85..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  49222 MW;  85155F7048E61D69 CRC64;
     MTTATAQQFR LPDLGEGLTE AGLVQWLVQV GDTIATDQAI AEVETAKSVV ELPSPFAGVV
     TALHGEPGET IAVGAVVLEV SANDAAPSHT ATPSQAEKEA YRAEERAGSG NVLIGYGTSE
     RAGSGRRRPR AASPASPPSA PDAVERTASA RSQAVHSTTS GALDDSSARR PVAVRSPLVR
     RLARELGVDV QTVTGSGADG AITRGDVLRA AVDHAVDGAA TPTASDQPAS AVSSTEIDGL
     AVRCREKLSP LRKAVSAKLS RSRAEIPEAT VWVDVDATRL WDARAEMASD GEKAPSLTAL
     VARFAVIALG DFPLLASRLS DDASELISFD GVNLGVAADT ERGLLVPVIP NAHTLSVAEF
     DRSLRDLAET ARSGTMPPER LRGSTFTLNN YGGFGVDGSA AIINHPDVAI LGIGRMMERP
     WVVDGEIVAR RIAQLSLVFD HRVCDGGYAA GFLRRVVELI EHPLRAYGRI
//