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Database: UniProt
Entry: U5LAF2_9BACI
LinkDB: U5LAF2_9BACI
Original site: U5LAF2_9BACI 
ID   U5LAF2_9BACI            Unreviewed;       445 AA.
AC   U5LAF2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=N288_08795 {ECO:0000313|EMBL:AGX03681.1};
OS   Bacillus infantis NRRL B-14911.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1367477 {ECO:0000313|EMBL:AGX03681.1, ECO:0000313|Proteomes:UP000017805};
RN   [1] {ECO:0000313|EMBL:AGX03681.1, ECO:0000313|Proteomes:UP000017805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-14911 {ECO:0000313|EMBL:AGX03681.1,
RC   ECO:0000313|Proteomes:UP000017805};
RA   Massilamany C., Smith T.P.L., Loy J.D., Barletta R., Reddy J.;
RT   "Complete genome sequence of Bacillus infantis NRRL B-14911 that has
RT   potential to induce cardiac disease by antigenic mimicry.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP006643; AGX03681.1; -; Genomic_DNA.
DR   RefSeq; WP_009791092.1; NC_022524.1.
DR   AlphaFoldDB; U5LAF2; -.
DR   STRING; 1367477.N288_08795; -.
DR   GeneID; 85551693; -.
DR   KEGG; bif:N288_08795; -.
DR   PATRIC; fig|1367477.3.peg.1690; -.
DR   HOGENOM; CLU_016733_10_0_9; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000017805; Chromosome.
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:UP000017805};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          142..179
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          84..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  47728 MW;  17036AC26F93E6DB CRC64;
     MSFQFRLPDI GEGIHEGEIV KWFIKPGDKV QEDDVLCEVQ NDKSVVEIPS PVEGTVEEVH
     ISEGTVATVG QVLVSFDAPG YEDLQFKGEH GDEAPAEKTE AQVQSTMEAG QDVKKEEAPG
     QEDAGKGTVI SQPDVDPDRR IIAMPSVRKF ARDKGVDIRQ VAGSGKNGRV LKEDIESFLN
     GGSQAPAQEA PQAEAAKEEA AAPAAAAAPQ GQYPETREKM SGIRKAIAKA MVNSKQTAPH
     VTLMDEIDVT KLVAHRKKFK EVAANKGIKL TFLPYVVKAL TSALREFPAL NTSIDDAAGE
     IIHKHYYNIG IAADTEKGLL VPVVKDADRK STFAISDEIN SLATKARDGK LAADEMKGAS
     CTITNIGSAG GQWFTPVINH PEVAILGIGR IAEKPVVKDG EIVAAPVLAL SLSFDHRIID
     GATAQNALNH IKRLLNDPEL LLMEA
//
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