ID W2US35_9FLAO Unreviewed; 432 AA.
AC W2US35;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=P278_04160 {ECO:0000313|EMBL:ETN96990.1};
OS Zhouia amylolytica AD3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zhouia.
OX NCBI_TaxID=1286632 {ECO:0000313|EMBL:ETN96990.1, ECO:0000313|Proteomes:UP000018850};
RN [1] {ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|Proteomes:UP000018850};
RA Jin H., Jeon C.O.;
RT "Draft genome sequence from a member of Zhouia, isolated tidal flat.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN96990.1, ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|EMBL:ETN96990.1,
RC ECO:0000313|Proteomes:UP000018850};
RX PubMed=27151796;
RA Jia B., Jin H.M., Lee H.J., Jeon C.O.;
RT "Draft Genome Sequence of Zhouia amylolytica AD3, Isolated from Tidal Flat
RT Sediment.";
RL Genome Announc. 4:0-0(2016).
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:ETN96990.1}.
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DR EMBL; AYXY01000001; ETN96990.1; -; Genomic_DNA.
DR RefSeq; WP_038261449.1; NZ_AYXY01000001.1.
DR AlphaFoldDB; W2US35; -.
DR STRING; 376730.SAMN04487906_2712; -.
DR PATRIC; fig|1286632.3.peg.416; -.
DR eggNOG; COG0508; Bacteria.
DR Proteomes; UP000018850; 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|RuleBase:RU003423,
KW ECO:0000313|EMBL:ETN96990.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000018850};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ETN96990.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 127..167
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 432 AA; 47247 MW; CBC064CD476800D1 CRC64;
MAKFELKLPK MGESVAEATI TSWLKEVGDT IEADEAVLEI ATDKVDSEVP SEVEGVLVER
FFEVDDVVQV GQVLAVIEIE GDAPAESNVA EPEEQMEEAV SELEESMESA KATVATTKVD
FSASDRFYSP LVKNMAKEEG IDVMELDTIQ GTGKDGRVTK NDMLAYIENR KSGQAIKSKT
TKPVAPIAPS VPVSVNGEDE IIEMTRMGKL IAHHMTESKH TSAHVQSFIE VDVTKIVNWR
NKIKKSFEQK EGEKLTFTPI FMEAIAKAIR DFPLINISVD GDKIIIKKNI NLGMAAALPD
GNLIVPVIKN ADRLNLVGMA KAVNDLAGRA RLNQLKPDEI QGGTYTVTNV GTFGSVFGTP
IINQPQVAIL ALGAIRKVPA VIETPDGDFI GIRHKMFLSH SYDHRVVNGA LGGQFVKRVA
EYLESWDSER EV
//
