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Database: UniProt
Entry: A0A2T0R759_9ACTN
LinkDB: A0A2T0R759_9ACTN
Original site: A0A2T0R759_9ACTN 
ID   A0A2T0R759_9ACTN        Unreviewed;       425 AA.
AC   A0A2T0R759;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=CLV37_103405 {ECO:0000313|EMBL:PRY16970.1};
OS   Kineococcus rhizosphaerae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Kineococcus.
OX   NCBI_TaxID=559628 {ECO:0000313|EMBL:PRY16970.1, ECO:0000313|Proteomes:UP000238083};
RN   [1] {ECO:0000313|EMBL:PRY16970.1, ECO:0000313|Proteomes:UP000238083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19711 {ECO:0000313|EMBL:PRY16970.1,
RC   ECO:0000313|Proteomes:UP000238083};
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:PRY16970.1}.
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DR   EMBL; PVZF01000003; PRY16970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0R759; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000238083; 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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:PRY16970.1};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:PRY16970.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          141..178
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          109..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..138
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   425 AA;  44974 MW;  21EF5113DBC94001 CRC64;
     MNQRFALPDV GEGLTEAEIV SWKVKPGDVV AVNDVLVEIE TAKSLVELPS PWAGTVTELL
     VAEGDTVDVG AHIVVVSDGT AAQAAAEPAA PQVDEALGAT LVGYGAKEAA PRRRRGAAPE
     VPPAQPQTQT PAPVPVQPHV LAKPPVRKLA RDLGIDLAGA RPTGPGGTVT RADVLALVPA
     APAEPERRFE KHERERHVPI RGVRKATAAA MVESAFSAPH VTVFTTVDAT RTMKLVQRLK
     TDPEYAGIRV SPLLLVAKAL LVAVRRNPDI NSTWDEKNQV IVVKNYVNLG IAVATPRGLL
     VPNVKDADEM SLKDLAVHLN DLALTAREGK AKPRDLAEGT ITITNVGTFG IDTGTPILNP
     GEAAILAVGK ISQRPWVHKG KVKPRYLATL GLSIDHRMLD GESGSRALAD IAAVLEDPAR
     ALTWS
//
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