ID A0A2V4MZA4_9ACTN Unreviewed; 430 AA.
AC A0A2V4MZA4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=C7C46_20955 {ECO:0000313|EMBL:PYC76908.1};
OS Streptomyces tateyamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=565073 {ECO:0000313|EMBL:PYC76908.1, ECO:0000313|Proteomes:UP000248039};
RN [1] {ECO:0000313|EMBL:PYC76908.1, ECO:0000313|Proteomes:UP000248039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21389 {ECO:0000313|EMBL:PYC76908.1,
RC ECO:0000313|Proteomes:UP000248039};
RA Schwalen C.J., Hudson G.A., Mitchell D.A.;
RT "Bioinformatic expansion and discovery of thiopeptide antibiotics.";
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:PYC76908.1}.
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DR EMBL; PYBW01000080; PYC76908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4MZA4; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000248039; 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:UP000248039};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 146..183
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 430 AA; 44710 MW; BB24BF05850CF75B CRC64;
MPIVREFTLP DLGEGLTGAE VVRWLVEVGE VIAVDQPVVE VETAKAVVEV PCPYGGVVTA
RFGEEGEERL VGQPLVTVAV SPEPGTDVPD PQPERPLVGY GVAEGGKGAR RRRLGATAVA
ASAAAAPAVA PAVAPAVVAA PAVVPVISPL VRKLAREHAV DLGSLTGSGP DGLIMRADVN
RAIETAAVPV AAPAVPSSPD SVPLRGLRRT VAEKLTRSHH EIPAATCWVD ADATELLAIR
AQMNQADAPK VSLLALLARI CVAALARYPE LNTSVDLDAN GAPAAIRRHP AVHLGFAAQS
DRGLVVPVVR DAQQLTTEQL GAELGRLTAA ARSGSLTPAE LTGGTFTLNN YGVFGVDGST
PILNHPEAAM LGVGRIIAKP WVHEGRLAVR QVTQLSFTFD HRVCDGGTAG GFLRFVADCL
ERPGMLLRQV
//