ID A0A367B5P9_9ACTN Unreviewed; 464 AA.
AC A0A367B5P9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=DQ237_05445 {ECO:0000313|EMBL:RBY97042.1};
OS Blastococcus sp. TF02-8.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=2250574 {ECO:0000313|EMBL:RBY97042.1, ECO:0000313|Proteomes:UP000252403};
RN [1] {ECO:0000313|EMBL:RBY97042.1, ECO:0000313|Proteomes:UP000252403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02-8 {ECO:0000313|EMBL:RBY97042.1,
RC ECO:0000313|Proteomes:UP000252403};
RA Ennis N., Dharumadurai D., Sevigny J., Hall J., Morris K., Simpson S.,
RA Thomas W.K., Tisa L.S.;
RT "Genome Sequence of Blastococcus sp. TF02-8.";
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:RBY97042.1}.
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DR EMBL; QOHK01000002; RBY97042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367B5P9; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000252403; 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 Reference proteome {ECO:0000313|Proteomes:UP000252403};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 7..82
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 181..218
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 102..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 47801 MW; 2E7050018BECE039 CRC64;
MTQTSTLRSF PLPDVGEGLT EGEILQWLVA VGDTVTVNQP LCEVETAKAA VELPSPWAGT
VVELLHEAGT TVDVGSPIIT IDVGGGAEPN GRTAVLVGYG PRTTEARRRP RRAAAEPAGS
PVVPPVSDDA PPLLATAPDM RTKPVRHGGL EVGRQAEAAA LSAAAAPARE AVPGRRGPRP
LAKPPVRKYA KGLGIDLTTL TGSGAGGCIT RADVDAALAA RSTAAAPPAV DDAAGQRIPI
KGVRRATAAA MVSSAFTAPH VTEFLTVDVT RMMKLRSRLA ARPELAGVKV SPLLFVAKAL
LLVAKRYPML NSSWDEAAQE IVVHGQVNLG IAAATPRGLV VPNIKDAGRL SLAELGAALG
ELTSTARAGR TSPADMAGGT LTITNVGVFG VDTGTPILNP GEAAILAFGT VREMPWVHKG
EVRPRQVTTL ALSFDHRIVD GELGSKALAD LGSLLHDPAT AIAY
//
