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
//