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
//