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Database: UniProt
Entry: S0JBJ4_9ENTE
LinkDB: S0JBJ4_9ENTE
Original site: S0JBJ4_9ENTE 
ID   S0JBJ4_9ENTE            Unreviewed;       534 AA.
AC   S0JBJ4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=OMQ_01045 {ECO:0000313|EMBL:EOT29732.1};
OS   Enterococcus saccharolyticus subsp. saccharolyticus ATCC 43076.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1139996 {ECO:0000313|EMBL:EOT29732.1, ECO:0000313|Proteomes:UP000014136};
RN   [1] {ECO:0000313|EMBL:EOT29732.1, ECO:0000313|Proteomes:UP000014136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43076 {ECO:0000313|EMBL:EOT29732.1,
RC   ECO:0000313|Proteomes:UP000014136};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus saccharolyticus ATCC_43076 (Illumina
RT   only assembly).";
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:EOT29732.1}.
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DR   EMBL; AHYT01000003; EOT29732.1; -; Genomic_DNA.
DR   RefSeq; WP_016174843.1; NZ_KE136523.1.
DR   AlphaFoldDB; S0JBJ4; -.
DR   STRING; 41997.RV16_GL002190; -.
DR   PATRIC; fig|1139996.3.peg.1029; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_9; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000014136; 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; 2.
DR   Gene3D; 2.40.50.100; -; 2.
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; 2.
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; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
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:UP000014136};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EOT29732.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          109..184
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          222..259
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          190..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  56180 MW;  625D894BA6BBEB19 CRC64;
     MAFQFKLPDI GEGIAEGEIV KWFVKPGDTI NEDDTLLEVQ NDKSVEEIPS PVTGTVKSIL
     VEEGVVANVG DVLVEIDAPG YEDEAPAAPA QEQTPAAPAA LPEAGGQGVF QFKLPDIGEG
     IAEGEIVKWF VKAGDTINED DTLLEVQNDK SVEEIPSPVT GTVVRVVVAE GVVANVGDVL
     VEIDAPGHNN APAAAPAQEA AAPASAPAEA AAPTGKPSKN VLAMPSVRQF ARENDVDITL
     VTPSGKGGRV TKEDIQSFIS GGSVAPAAPA QEAAAPVAEA KPAAKEEKAA PAKPYSSDLG
     ALETREKLTP MRKAISKAMV NSKHTAPHVT LHDEVEVSKL WDQRKKFKDV AAAQNTKLTF
     LPYVVKALTA TMKKYPVLNA SIDDAAQEVV YKNYYNIGIA TDTANGLYVP NVKDADRKGL
     FAIADEINGK AALAHEGKLA AEDMRNGTVT ISNIGSVGGA WFTPVINYPE VAILGVGTIA
     QQPVVNAEGE IVVGRMMKLS LSFDHRIVDG ATAQQAMNNI KRLLADPELL LMEG
//
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