ID M8EE02_9BACL Unreviewed; 465 AA.
AC M8EE02;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=I532_06790 {ECO:0000313|EMBL:EMT53700.1};
OS Brevibacillus borstelensis AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT53700.1, ECO:0000313|Proteomes:UP000012081};
RN [1] {ECO:0000313|EMBL:EMT53700.1, ECO:0000313|Proteomes:UP000012081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT53700.1,
RC ECO:0000313|Proteomes:UP000012081};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL Submitted (MAR-2013) 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:EMT53700.1}.
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DR EMBL; APBN01000002; EMT53700.1; -; Genomic_DNA.
DR RefSeq; WP_003387219.1; NZ_APBN01000002.1.
DR AlphaFoldDB; M8EE02; -.
DR STRING; 1300222.I532_06790; -.
DR GeneID; 72734520; -.
DR PATRIC; fig|1300222.3.peg.1394; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000012081; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000012081};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EMT53700.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 150..187
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 48970 MW; 51269BE09B4937AB CRC64;
MATKVLMPQL GESVTEGTIT KWLVKVGDQV KKYDPLAEVS TDKVNAEVPS TVAGRVTEIV
VPEGDTVAIG TLILYIEEEG GGADQPENTP AVNSADTSQQ AKTVPAQAAE GRAAVSANLA
ANAAPTAAGQ AVSGVGPDTN GQQAQRGKQR FSPAVMRLAQ EHGIDLSRVQ GTGMEGRVTR
KDIQAIIDNG GQPAAAAPEA APVVNTPVGV PASAAVGQSP QPVQAAAREV PAAAGDQIIP
VTPIRKTIAN RMVQSKHEAP HAWTMVEVDV TKLVAFRNQV KDEFKRKEGV NLTFLPFFIK
AVVEALKEYP MINSTWAGDK IIVKKNINIS IAVATEDALF VPVIKDADQK SILGIAKSIE
DLAAKTRAGK LSVDDMSGGT FTVNNTGSFG SVLSMPIINS PQAAILSVES IVKRPVVIDD
MIAVRSMVNL CLSLDHRVLD GLVCGRFLQS VKQKLEAIGP DTKLY
//
