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Database: UniProt
Entry: A0A0M2GXQ4_9ACTN
LinkDB: A0A0M2GXQ4_9ACTN
Original site: A0A0M2GXQ4_9ACTN 
ID   A0A0M2GXQ4_9ACTN        Unreviewed;       475 AA.
AC   A0A0M2GXQ4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=UK15_08215 {ECO:0000313|EMBL:KJK40309.1};
OS   Streptomyces variegatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=284040 {ECO:0000313|EMBL:KJK40309.1, ECO:0000313|Proteomes:UP000034786};
RN   [1] {ECO:0000313|Proteomes:UP000034786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16380 {ECO:0000313|Proteomes:UP000034786};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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:KJK40309.1}.
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DR   EMBL; JYJH01000004; KJK40309.1; -; Genomic_DNA.
DR   RefSeq; WP_031137523.1; NZ_JYJH01000004.1.
DR   AlphaFoldDB; A0A0M2GXQ4; -.
DR   STRING; 284040.UK15_08215; -.
DR   PATRIC; fig|284040.3.peg.4936; -.
DR   Proteomes; UP000034786; 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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          4..79
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          86..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  49196 MW;  58F00C63EF581956 CRC64;
     MAQVLEFKLP DLGEGLTEAE IVRWLVEVGD VVAIDQPVVE VETAKAMVEV PCPYGGVVTA
     RFGEEGTELP VGAPLITVAV GERPATGAGD AGSEGSGNVL VGYGTSEAPA RRRRVRQERP
     VPGPSATTGQ AGAAGRVNGR ADAAASPVNA QAAGAAPVKA QGDGLATEDG PVPVISPLVR
     RLARQNGLDL RELTGRGPDG LILRADVEYA LRAAGQGATA APAAEPHPRV PRASAPQPSV
     ASAAGPGEIR TPLKGVRGAV ADKLARSRRE IPDATCWVDA DATELMRART AMNAAGGPKI
     SLLALLARIC TAALARFPEL NATVDAEARE IVRFDHVHLG FAAQTDRGLV VPVVRDAHAR
     DAESLTAEFA RLTEAGRTGA LTPGELTGGT FTLNNYGVFG VDGSTPIINH PEAAMLGVGR
     IVPKPWVHEG ELAVRQVVQL SLTFDHRVCD GGVAGGFLRY VADCVEQPAV LLRTL
//
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