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Database: UniProt
Entry: A0A2V2PZW9_9ACTN
LinkDB: A0A2V2PZW9_9ACTN
Original site: A0A2V2PZW9_9ACTN 
ID   A0A2V2PZW9_9ACTN        Unreviewed;       476 AA.
AC   A0A2V2PZW9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=DKT74_09845 {ECO:0000313|EMBL:PWS45192.1};
OS   Streptomyces sp. ZEA17I.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2202516 {ECO:0000313|EMBL:PWS45192.1, ECO:0000313|Proteomes:UP000245984};
RN   [1] {ECO:0000313|EMBL:PWS45192.1, ECO:0000313|Proteomes:UP000245984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZEA17I {ECO:0000313|EMBL:PWS45192.1,
RC   ECO:0000313|Proteomes:UP000245984};
RA   Chen X., Qin K., Li H., Cortesi P., Saracchi M., Sang W., Yang M.;
RT   "Genome sequencing and identification of chitinase family genes of
RT   Streptomyces sp. ZEA17I, a biocontrol agent against plant pathogens.";
RL   Submitted (MAY-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:PWS45192.1}.
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DR   EMBL; QGMS01000714; PWS45192.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V2PZW9; -.
DR   Proteomes; UP000245984; 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   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          11..86
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          177..214
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          91..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  49437 MW;  B8A377CD2C83EF1C CRC64;
     MTTMTQTSAR FREFKMPDVG EGLTEAEILK WFVQPGDTVT DGQVVCEVET AKAAVELPIP
     FDGVVHELRF GEGTTVDVGQ VIITVDVAPG SAEEAPPAPA VQEPVEAPAP AAPASDEPKG
     RTPVLVGYGV AESSTKRRPR KGAAPEAAAV AAAVQAELNG HGAPAAPEPE VPVTRPLAKP
     PVRKLAKDLG VDLASVVPTG KDGIITREDV HAAAAPAQAA APAPVPAAEP VTVAVDKAEA
     TVSARETRIP IKGVRKAIAQ AMVGSAFTAP HVTEFVTVDV TRTMKLVAEL KEDKDMAGVR
     VNPLLVIAKA LLVAIKRNPG VNAAWDEANQ EIVQKHYVNL GIAAATPRGL IVPNIKDAHD
     KTLPQLAEAL GELVATARDG KTSPAAMAGG TVTITNVGVF GVDTGTPILN PGESAILAVG
     AIKLQPWVHK GKVKPRQVTT LALSFDHRLV DGELGSKVLA DVAAILEQPK RLITWA
//
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