ID A0A2Z4V8W1_9ACTN Unreviewed; 479 AA.
AC A0A2Z4V8W1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-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=DRB96_03525 {ECO:0000313|EMBL:AWZ17708.1};
OS Streptomyces sp. ICC1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2099583 {ECO:0000313|EMBL:AWZ17708.1, ECO:0000313|Proteomes:UP000250268};
RN [1] {ECO:0000313|EMBL:AWZ17708.1, ECO:0000313|Proteomes:UP000250268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC1 {ECO:0000313|EMBL:AWZ17708.1,
RC ECO:0000313|Proteomes:UP000250268};
RA Gosse J.;
RT "Whole genome sequencing and metabolomic study of cave Streptomyces
RT isolates ICC1 and ICC4.";
RL Submitted (JUN-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}.
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DR EMBL; CP030287; AWZ17708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4V8W1; -.
DR Proteomes; UP000250268; 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; 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:UP000250268};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 1..71
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 174..211
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 223..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 49098 MW; 1F8FF61109FEE286 CRC64;
MPDVGEGLTE AEILKWYVQP GDTVTDGQVV CEVETAKAAV ELPIPFDGVV HALLFEEGVT
VDVGQVIISV QTGPADEAPA AAVAAAPVAA APVAAEAEPE APAARQPVLV GYGVSTASTK
RRPRKAPQPA VAARNGTGVA QAAPAAAAPA APAVVVPAVV LPAQNGTGSG ARALAKPPVR
KLAKDLGIDL AVVVPTGDGG VVTREDVHAA AAAAIAPQAL APAPEAPPVQ AQAQAPASAP
AEAPASARET RIPVKGVRKI TAQAMVGSAF TAPHVTEFIT FDVTRTMKLV QELKADPDLA
GLRINPLLLI AKAVLVAVRR NPEVNASWDE AAQEIVLKHY VNLGIAAATP RGLIVPNIKD
AHAKTLPELS TALSELVATA REGKTSPADM QNGTITLTNV GVFGVDTGTP ILNPGESAIL
AVGAIKLQPW VHKGKVKARQ VTTLALSFDH RLIDGELGSR FLADIAAVLE HPRRLITWS
//
