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Database: UniProt
Entry: E2YWX1_ENTFL
LinkDB: E2YWX1_ENTFL
Original site: E2YWX1_ENTFL 
ID   E2YWX1_ENTFL            Unreviewed;       539 AA.
AC   E2YWX1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=HMPREF9512_01851 {ECO:0000313|EMBL:EFQ15856.1};
OS   Enterococcus faecalis EnGen0311.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=749509 {ECO:0000313|EMBL:EFQ15856.1, ECO:0000313|Proteomes:UP000004414};
RN   [1] {ECO:0000313|EMBL:EFQ15856.1, ECO:0000313|Proteomes:UP000004414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX0635 {ECO:0000313|EMBL:EFQ15856.1,
RC   ECO:0000313|Proteomes:UP000004414};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2010) 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:EFQ15856.1}.
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DR   EMBL; AEBZ01000042; EFQ15856.1; -; Genomic_DNA.
DR   RefSeq; WP_002357766.1; NZ_KB947266.1.
DR   AlphaFoldDB; E2YWX1; -.
DR   PATRIC; fig|749509.5.peg.1256; -.
DR   BioCyc; EFAE749509-HMP:GMEG-888-MONOMER; -.
DR   Proteomes; UP000004414; Unassembled WGS sequence.
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   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EFQ15856.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          112..187
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          230..267
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          79..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   539 AA;  56633 MW;  9B9B10E1C496151B CRC64;
     MAYQFKLPDI GEGIAEGEIV KWFVKPGDTI NEDDTLLEVQ NDKSVEEIPS PVTGTVKNIV
     VPEGTVANVG DVLIEIDAPG HEDNDAAPAA PAQEQTPAQP AAVPTTEAAG GFFQFKLPDI
     GEGIAEGEIV KWFVKAGDTI NEDDSLLEVQ NDKSVEEIPS PVTGTVKNIV VPEGTVANVG
     DVLVEIDAPG HNSAAPAAAA PATDAPKAEA SAPAASTGVV AAADPNKRVL AMPSVRQYAR
     EKDVDITQVT ATGKGGRVIK ADIDAFVSGG SQAAPATEAA ATEAAPKAEA AAPKAAPKAF
     TSDLGEMETR EKMTPTRKAI AKAMVNSKHT APHVTLHDEV EVSKLWDHRK KFKDVAAANG
     TKLTFLPYVV KALTSTVQKF PILNASIDDA AQEIVYKNYF NIGIATDTDH GLYVPNVKNA
     NTKSMFAIAD EINEKAALAI EGKLTAQDMR DGTITISNIG SVGGGWFTPV INYPEVAILG
     VGTIAQEPVV NADGEIVVGR MMKLSLSFDH RIVDGATAQK AMNNIKRLLA DPELLLMEG
//
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