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Database: UniProt
Entry: W7AWG2_9LIST
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ID   W7AWG2_9LIST            Unreviewed;       432 AA.
AC   W7AWG2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=MAQA_11106 {ECO:0000313|EMBL:EUJ17575.1};
OS   Listeria aquatica FSL S10-1188.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1265818 {ECO:0000313|EMBL:EUJ17575.1, ECO:0000313|Proteomes:UP000019246};
RN   [1] {ECO:0000313|EMBL:EUJ17575.1, ECO:0000313|Proteomes:UP000019246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL S10-1188 {ECO:0000313|EMBL:EUJ17575.1,
RC   ECO:0000313|Proteomes:UP000019246};
RX   PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA   den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA   Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA   Nightingale K.K., Kephart D., Wiedmann M.;
RT   "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT   cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT   sp. nov., from agricultural and natural environments.";
RL   Int. J. Syst. Evol. Microbiol. 64:1882-1889(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:EUJ17575.1}.
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DR   EMBL; AOCG01000012; EUJ17575.1; -; Genomic_DNA.
DR   RefSeq; WP_036073355.1; NZ_AOCG01000012.1.
DR   AlphaFoldDB; W7AWG2; -.
DR   STRING; 1265818.MAQA_11106; -.
DR   PATRIC; fig|1265818.5.peg.2230; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000019246; Unassembled WGS sequence.
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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EUJ17575.1}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          125..162
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          81..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  46784 MW;  DDD180918ADBE7D7 CRC64;
     MAIMEITMPK LGESVTEGTI SSWLVEPGQK VEKYDAIAEV LTDKVTAEVP SSYSGTIKEL
     IAKEDETLEV GAVICTIETE EAGETQDAAS TEERAPTKEV ESAQLSQSSG GNIQQAKANA
     PSGARLSPAV LRLSAEHGVD LNQVEGSGKG GRITRKDILQ FVESGGASSE KQVAQSETPA
     VTSSSPKQEK EAVQVPKAAN GDREIPVSGV RKAIAKHMVE SKHEIPHAWM MTEADATSLV
     RYRNSLKDKF KQEEGFSLTY FAFFIKAVAQ TLKEFPTLNS TWATDKIIEH KDVNISIAIA
     ANDLLYVPVI KNADEKSIKG IAREISELAA KARNNKLTQE DMSGGTFTVN STGSFGSVQS
     MGIINHPQAA ILQVESIVKR PVVINDMIAI RDMVNLCLSI DHRILDGLMA GRFLQAIKKK
     VEEISKDNTP IY
//
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