ID A0A0Q4FLP5_9SPHI Unreviewed; 452 AA.
AC A0A0Q4FLP5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=ASE74_09695 {ECO:0000313|EMBL:KQM66149.1};
OS Pedobacter sp. Leaf216.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1735684 {ECO:0000313|EMBL:KQM66149.1, ECO:0000313|Proteomes:UP000051744};
RN [1] {ECO:0000313|Proteomes:UP000051744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA Garrido-Oter R., Mueller D.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQM66149.1}.
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DR EMBL; LMKM01000035; KQM66149.1; -; Genomic_DNA.
DR RefSeq; WP_055913850.1; NZ_LMKM01000035.1.
DR AlphaFoldDB; A0A0Q4FLP5; -.
DR STRING; 1735684.ASE74_09695; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000051744; 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; 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 Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 128..168
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 452 AA; 48822 MW; D25389F649C4B1F7 CRC64;
MAQYELLLPK MGESVAEATV IKWVKQPGDS IELDDTILEI ATDKVDSEVP SPVAGKLVKQ
LFAADEVAQV GDVIAIIETE GGDISKDETP VVEKPVAEEK TETIPGIEQL PIANQPAATT
DFSTSERFYS PLVKSIAAQE NISIAELDAI KGSGADGRLN KDDLLDYIAR KNGDVVKTAT
VIITPPVPPV NEVAAHKTEA TNQAPIANKP STTSVNGADE IIEMDRMRKL IADHMVMSKT
TSPHVTSFVE ADVTNMVLWR NKVKNSFEKR ENEKITFTPI FVEAVAKAIK DFPMINVSVN
GTQIIKKGNI NIGMAAALPS GNLIVPVIRN ADQLNLVGLT KAVNDLAGRA RNSKLKPDET
QGGTFTLTNV GSFGNVMGTP IINQPQVAIL AVGAIKKKPA VLETEHGDVI AIRHMMFLSL
SYDHRVVDGS LGGMFVRRVA DYLEGWDLNR EI
//