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Database: UniProt
Entry: A0A0V8JDB5_9BACI
LinkDB: A0A0V8JDB5_9BACI
Original site: A0A0V8JDB5_9BACI 
ID   A0A0V8JDB5_9BACI        Unreviewed;       432 AA.
AC   A0A0V8JDB5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=AS030_05195 {ECO:0000313|EMBL:KSU84922.1};
OS   Fictibacillus enclensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU84922.1, ECO:0000313|Proteomes:UP000054099};
RN   [1] {ECO:0000313|EMBL:KSU84922.1, ECO:0000313|Proteomes:UP000054099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU84922.1,
RC   ECO:0000313|Proteomes:UP000054099};
RX   PubMed=24343101; DOI=10.1007/s10482-013-0097-9;
RA   Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C.,
RA   Ramana V.V., Shouche Y.S.;
RT   "Fictibacillus enclensis sp. nov., isolated from marine sediment.";
RL   Antonie Van Leeuwenhoek 105:461-469(2014).
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:KSU84922.1}.
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DR   EMBL; LNQN01000001; KSU84922.1; -; Genomic_DNA.
DR   RefSeq; WP_061969140.1; NZ_KQ758617.1.
DR   AlphaFoldDB; A0A0V8JDB5; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000054099; 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:UP000054099};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          131..168
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          76..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  46746 MW;  37401F572E327EB7 CRC64;
     MAFEFKLPDI GEGIHEGEIV KWFVKAGDEV KEDDILLEVQ NDKAVVEIPS PVDGKILEVK
     VDEGTVSVVG DVLVTIESDS APESEETEEA PEQPKADEEQ KPAAAEPEQK TEAAKTEPSA
     DELVDENKRV IAMPSVRKYA REKGVDIRKV SGSGDNGRVM KEDIEKFLSG DTTSQDQEAV
     TAPAEAPAAK EAPKAIPAGQ NETREKIKGV RKIIAKAMVN SKHTAPHVTL MDEIDVTELV
     AHRKKFKQVA ADKGIKLTYL PYVVKALVSA AREFPAINAS IDDANEEIVW KNYYNIGIAA
     DTDNGLMVPV VKDADRKSIF KISAEINELA VKARDGKLSA DEMKGGSVTI SNIGSAGGQW
     FTPVINHPEV AILGIGRIAE KAVVKNGEIV VAPVLALSLS FDHRLIDGVT AQNAMNHIKR
     LLNDPQLLVM EA
//
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