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Database: UniProt
Entry: A0A368W689_9BACL
LinkDB: A0A368W689_9BACL
Original site: A0A368W689_9BACL 
ID   A0A368W689_9BACL        Unreviewed;       445 AA.
AC   A0A368W689;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=DFP97_102130 {ECO:0000313|EMBL:RCW50938.1};
OS   Paenibacillus prosopidis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=630520 {ECO:0000313|EMBL:RCW50938.1, ECO:0000313|Proteomes:UP000252415};
RN   [1] {ECO:0000313|EMBL:RCW50938.1, ECO:0000313|Proteomes:UP000252415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7506 {ECO:0000313|EMBL:RCW50938.1,
RC   ECO:0000313|Proteomes:UP000252415};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-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:RCW50938.1}.
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DR   EMBL; QPJD01000002; RCW50938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368W689; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000252415; 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|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:RCW50938.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252415};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:RCW50938.1}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          135..172
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          86..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  46726 MW;  5439ED43A44B16F2 CRC64;
     MAKFEYRFPE LGEGLHEGEI IKVLIKVGDT VTDDDIIMEV QNDKAIVEVP CPVNGKVLEV
     LVKDGQVCHV GEIVAIIDAE GELPEQAAPA AEAPKAEAPA AAAPAAAPEA PAAPAAQAAA
     PTAAAAPKAT GGLVLATPSV RKFAREKGVD LTQVGGTGKN GRITRDDVTG FGGAPAAVAA
     DTAAPAAVEQ QDNAAKVAGE AKAAPVTAGT AYRPEERVPF KGIRKIIANA MTKSVYTAPH
     VTIMDEVDVT ELVALRAKYK PYAEKKGSKL TYLPFIVKAL VAACREFPIL NATLDEANQE
     IVLRKYYNIG IATDTDNGLI VPVIEDADRK NLFKIADSIR DLAARGRDGK LAANELKGST
     ISISNIGSAG GMFFTPVINF PEVAILGTGR ITEKAIVRNG EIVAAPVMAL SLSFDHRLID
     GATAQNFMNY IKTLLGQPEL FIMEV
//
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