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Database: UniProt
Entry: A0A2M8MBJ9_9ACTN
LinkDB: A0A2M8MBJ9_9ACTN
Original site: A0A2M8MBJ9_9ACTN 
ID   A0A2M8MBJ9_9ACTN        Unreviewed;       444 AA.
AC   A0A2M8MBJ9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-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=CUT44_02575 {ECO:0000313|EMBL:PJF01560.1};
OS   Streptomyces carminius.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2665496 {ECO:0000313|EMBL:PJF01560.1, ECO:0000313|Proteomes:UP000230407};
RN   [1] {ECO:0000313|EMBL:PJF01560.1, ECO:0000313|Proteomes:UP000230407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRM SA0054 {ECO:0000313|EMBL:PJF01560.1,
RC   ECO:0000313|Proteomes:UP000230407};
RA   Wang Y., Luo X., Wan C., Zhang L.;
RT   "Streptomyces carmine sp. nov., a novel actinomycete isolated from Sophora
RT   alopecuroides in Xinjiang, China.";
RL   Submitted (NOV-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:PJF01560.1}.
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DR   EMBL; PGGW01000010; PJF01560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M8MBJ9; -.
DR   Proteomes; UP000230407; 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:UP000230407};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          4..79
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          165..202
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          119..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   444 AA;  45876 MW;  B03BEDFCFF301B5B CRC64;
     MPEVREFALP DLGEGLTEAE IVRWLVAVGE VVAVDQPVVE VETAKAVVEV PCPYGGVVTA
     RFGAEGDEVP VGAPLVTVAV GASAASAVHG AAGADEAGEP ERSGNVLVGY GTAAPAVRRR
     RLRPAPVPSG SALGDGHGDG LGDGPVPATG PAPVSTAPEP GTVPVISPLV RRLAREHGID
     LRRVPGSGPR GLILRADVER AVRAARTAAP APAPQGERIP LRGLRGAVAD KLTVSRREIP
     DATCWVDADA TELLAARRAM NEHGGGPEIS LLALLARICT AALARFPELN ATVDTAAREI
     VRLPAAHLGF AAQTERGLVV PVVRDAHARD TAALSAEIAR LTAAARAGRL KPAELTGGTF
     TLNNYGVFGV DGSTPIVNHP EAAMLGVGRI APKPWVHGGE LAVRRVVQLS LTFDHRVCDG
     GTAGGFLRYV ADRVEHPAVL LREM
//
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