ID A0A2S9QRD9_9MICO Unreviewed; 613 AA.
AC A0A2S9QRD9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=B4915_03635 {ECO:0000313|EMBL:PRI12156.1};
OS Leucobacter massiliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1686285 {ECO:0000313|EMBL:PRI12156.1, ECO:0000313|Proteomes:UP000238650};
RN [1] {ECO:0000313|EMBL:PRI12156.1, ECO:0000313|Proteomes:UP000238650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=122RC15 {ECO:0000313|EMBL:PRI12156.1,
RC ECO:0000313|Proteomes:UP000238650};
RX PubMed=29204283;
RA Leangapichart T., Gautret P., Nguyen T.T., Armstrong N., Rolain J.M.;
RT "Genome sequence of 'Leucobacter massiliensis' sp. nov. isolated from human
RT pharynx after travel to the 2014 Hajj.";
RL New Microbes New Infect 21:42-48(2017).
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:PRI12156.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MWZD01000013; PRI12156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9QRD9; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000238650; 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; 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; IPR014276; 2-oxoglutarate_DH_E2.
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 NCBIfam; TIGR02927; SucB_Actino; 1.
DR PANTHER; PTHR43416:SF8; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000238650};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:PRI12156.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 145..220
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 312..349
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 79..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 61595 MW; 51255032CFCA9C81 CRC64;
MSESVVLPAL GESVTEGTVT RWLKNVGDTV EVDEPLLEVS TDKVDTEIPS PVAGVLEEIL
VQEDETAEVG AVLATVGDGS GSGASAEAAA PAAASEAAPA AAPEPPAAPE PAAAPEPAAQ
AAPAAAQAAP AAAPQSEAAG SGGEGQEIVL PSLGESITEG TVTRWLKSVG DTVEVDEPLL
EVSTDKVDTE VPSPVAGVLQ EILVQEDDTV EVGGVLARVG GSAAGSADEA PAAAPEPAQQ
PEAPAAPAAE PAPAPAASEA PAQPSADADE AAPAQQASAP AHGAAPAEPA QPSAQAAPAA
PQASAPADAP GYLTPIVRKL AHERGVDLAS VRGTGVGGRI RKEDVLAAAE SARQSAAPAA
SQAQAAPAPA PAEVSPLRGT TQKMSRLRKV IAERAVASLQ GTAQLTTVVE VDVTRVARLR
QAKKDEFLAK TGSKLSFMPF FALAAAEALR SFPIINATVD GDSIVYPATE NISIAVDTEK
GLLTPVLRDA GDKNIAEIAG EIADLAARTR DNQLKPDELA GGTFTLTNTG SRGALFDTPL
VFLPQSAILG TGAVVKKPAV VSGPEGDAIA IRSTVYLALS YDHRIIDGAD AARFLGQLRA
RLEAGDFEAQ LGI
//
