ID A0A1V6MLD5_9ACTN Unreviewed; 494 AA.
AC A0A1V6MLD5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BM536_027670 {ECO:0000313|EMBL:OQD53290.1};
OS Streptomyces phaeoluteigriseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=114686 {ECO:0000313|EMBL:OQD53290.1, ECO:0000313|Proteomes:UP000184286};
RN [1] {ECO:0000313|Proteomes:UP000184286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41896 {ECO:0000313|Proteomes:UP000184286};
RA Schniete J.K., Salih T., Algora Gallardo L., Martinez Fernandez S.,
RA Herron P.R.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OQD53290.1, ECO:0000313|Proteomes:UP000184286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41896 {ECO:0000313|EMBL:OQD53290.1,
RC ECO:0000313|Proteomes:UP000184286};
RA Salih T.S., Algora Gallardo L., Melo Santos T., Filgueira Martinez S.,
RA Herron P.R.;
RT "Draft genome sequence of Streptomyces phaeoluteigriseus type strain
RT DSM41896.";
RL Submitted (FEB-2017) 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:OQD53290.1}.
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DR EMBL; MPOH02000017; OQD53290.1; -; Genomic_DNA.
DR RefSeq; WP_073498288.1; NZ_MPOH02000017.1.
DR AlphaFoldDB; A0A1V6MLD5; -.
DR STRING; 114686.BM536_027670; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000184286; 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 9..85
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 187..224
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 89..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 51266 MW; 5C5D1485B7F915A2 CRC64;
MTTMTEASVR EFKMPDVGEG LTEAEILKWY VQPGDTVTDG QVVCEVETAK AAVELPIPYD
GVVRELRFPE GTTVDVGTSI IAVDVSGGSA PAAAPAAPAP PATQEQPEEP KAEGSGRQPV
LVGYGVATSS TKRRPRKATE NPAQESEPVS AAVQAELNGH GTLPATATAT APPAPASAQA
VAAGRPLAKP PVRKLAKDLG VDLASVVPSG PDGIITREDV HAAAAAPEQA PAGPTAPQPM
PAGTPAPVTT AAPAPAASYD SGRETRIPVK GVRKATAQAM VGSAFTAPHV TEFVTIDVTR
TMKLVEELKR DKDMQGLRVN PLLLIAKALL VAIRRNPDVN ASWDEANQEI VRKHYVNLGI
AAATPRGLIV PNIKDAHDKT LPQLAEALGE LVATAREGRT SPAAMQGGTV TITNVGVFGV
DTGTPILNPG ESAILAVGAI KLQPWVHKGK VKPRQVTTLA LSFDHRLVDG ELGSKVLADV
AAVLEQPKRL ITWG
//
