ID A0A2T7QF44_9BACT Unreviewed; 458 AA.
AC A0A2T7QF44;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=DC498_00700 {ECO:0000313|EMBL:PVD53949.1};
OS Terrimonas sp.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Terrimonas.
OX NCBI_TaxID=1914338 {ECO:0000313|EMBL:PVD53949.1, ECO:0000313|Proteomes:UP000244333};
RN [1] {ECO:0000313|EMBL:PVD53949.1, ECO:0000313|Proteomes:UP000244333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS-102 {ECO:0000313|EMBL:PVD53949.1,
RC ECO:0000313|Proteomes:UP000244333};
RA Zhang L., Jiang J.;
RT "The draft genome of strain NS-102.";
RL Submitted (APR-2018) 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:PVD53949.1}.
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DR EMBL; QCZJ01000001; PVD53949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7QF44; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000244333; 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 Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000244333};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 132..172
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 181..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 49856 MW; 89096AA82D561648 CRC64;
MAIVDLVMPK LGESIIEATI LRWNKKPGDH VKIDETILEI ATDKVDSEVP SAVEGTLVEI
LYNENDVVPV DTVIARIQSE ANGTLPTVVP ATEAETGQTA KEDTEADDLV TKEVPYQPIH
IDIPKATGGA RFYSPLVLNI AANEGISLAE LENIPGTGND GRVTKKDILQ WVEKKKSDVV
NTPVQEPKVV TQSSATTQPA QSAQQSTQAT TPEAEKPAVA YDGNAEIIEM DRMRKLIAKH
MVESKQTSPH VTSFTECDVT NLVQWRDKIK ANFEKQEGEK ITFMPLFIEA IIKCIKKFPW
VNASVDGDKI IVKKDINIGM ATALPNGNLI VPVIKEADYL NLTGLTKKIN ALANAARNNR
LKPDDTQGGT FTVTNVGTFG TLMGTPIINQ PQVAILAIGA IKKRPVVVET AQGDSIAIRH
MMYLSMSYDH RIVDGSIGAS FLTAVANELE AFDTHRTI
//
