ID A0A0M4H5F2_9ACTO Unreviewed; 501 AA.
AC A0A0M4H5F2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=AM609_07305 {ECO:0000313|EMBL:ALC99340.1};
OS Actinomyces sp. oral taxon 414.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=712122 {ECO:0000313|EMBL:ALC99340.1, ECO:0000313|Proteomes:UP000061022};
RN [1] {ECO:0000313|Proteomes:UP000061022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0588 {ECO:0000313|Proteomes:UP000061022};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (AUG-2015) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012590; ALC99340.1; -; Genomic_DNA.
DR RefSeq; WP_053586747.1; NZ_CP012590.1.
DR AlphaFoldDB; A0A0M4H5F2; -.
DR STRING; 712122.AM609_07305; -.
DR KEGG; acq:AM609_07305; -.
DR PATRIC; fig|712122.3.peg.1650; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000061022; Chromosome.
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; IPR014276; 2-oxoglutarate_DH_E2.
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 NCBIfam; TIGR02927; SucB_Actino; 1.
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:ALC99340.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 186..223
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 80..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..173
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 50685 MW; DB664F8E8A8D348B CRC64;
MSESVKMPAL GESVTEGTVS SWLKAVGDSV EVDEPLLEVA TDKVDTEVPS PAAGTVLEIL
VPEDETVDVG TVLAIIGDPS EASPAPTPSI PAASAPAPAV AEPVQPAAAP AQPPAPAGPA
APAQSAPAPA GPAATAATPA VPATASAAIP AQPARPEPAP VQPAAPTGPA APAAAPAAPA
VASAAYVTPI VRKLARDKGV DLTAVSGTGV GGRIRKEDVQ KAAAQAEEAR RAAEARAAAA
SAAPAGPAAP APAAPTRPAV DTTLRGRTEK MSRLRQVIAE RMIDSLRTSA QLTTVVEVDV
TRVASLRARA KDGFLAKNGT KLTFLPFFVA AATEALKAHP KLNATIDGKQ VAYHDVEHIG
IAVDTPRGLL VPVVKNAGDL NIPGLARRIN DLAARTRASK VDPDELSGST FTITNTGSGG
ALFDTPIINQ PEVAILGLGA ITKQPRVVAD ADGNEAIAVR SVCHLSLSYD HRLVDGADAA
RYLMTVKKRL EEGDFAGELG L
//
