ID A0A2P8CAG1_9BACT Unreviewed; 442 AA.
AC A0A2P8CAG1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CLV93_10766 {ECO:0000313|EMBL:PSK81956.1};
OS Prolixibacter denitrificans.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Prolixibacter.
OX NCBI_TaxID=1541063 {ECO:0000313|EMBL:PSK81956.1, ECO:0000313|Proteomes:UP000240621};
RN [1] {ECO:0000313|EMBL:PSK81956.1, ECO:0000313|Proteomes:UP000240621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27267 {ECO:0000313|EMBL:PSK81956.1,
RC ECO:0000313|Proteomes:UP000240621};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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:PSK81956.1}.
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DR EMBL; PYGC01000007; PSK81956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8CAG1; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000240621; 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 Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:PSK81956.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 129..169
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 48044 MW; D38A07AB52A77B6C CRC64;
MSDFQVMMPK MGESVQEATI TKMFVKKGDT VEEDDVLFEI ATDKVDSEIP SPVAGKVKEI
KYNEDDLVAV GEVVMLISMD GEDEGDDTSS EETTDKKAEE QPAAKEEKSE TPKDSGAPQG
NVNKQSGRFY SPLVRSIADK EGVSFDELES IEGSGQGGRV QKKDILAYLE NRGSGKAAQP
AAASAPAQEA KAAPQAQQHK VSVSIGAEDT IVEMDRVRKM IADHMVTSKH VAPHVTSVVE
ADMTNMVLWR NKVKGEYQEK YGEKITFMPL ITEAVAKALA EFPYVNSSVD GYNIVLRKHV
NIGMAVATEN NNLVVPVIKD ADTKNLLGLT KDVNRLAALG RKNNLGPDDL QGGTFAITNF
GSFGNIIGTP IINQPQTAIL AVGTIEKKPA VMETPTGDAI VVRHKMFLSL SYDHRVIDGM
LGGKFLRRVA DILEEHDPNR EI
//
