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Database: UniProt
Entry: A0A1S1R061_9ACTN
LinkDB: A0A1S1R061_9ACTN
Original site: A0A1S1R061_9ACTN 
ID   A0A1S1R061_9ACTN        Unreviewed;       527 AA.
AC   A0A1S1R061;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=BCD49_11080 {ECO:0000313|EMBL:OHV39590.1};
OS   Pseudofrankia sp. EUN1h.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Pseudofrankia.
OX   NCBI_TaxID=1834515 {ECO:0000313|EMBL:OHV39590.1, ECO:0000313|Proteomes:UP000179465};
RN   [1] {ECO:0000313|Proteomes:UP000179465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EUN1h {ECO:0000313|Proteomes:UP000179465};
RA   Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA   Nouioui I., Abebe-Akele F., Thomas K., Gtari M., Tisa L.S.;
RT   "Sequence Frankia sp. strain EUN1h.";
RL   Submitted (JUL-2016) 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:OHV39590.1}.
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DR   EMBL; MBLN01000036; OHV39590.1; -; Genomic_DNA.
DR   RefSeq; WP_007516178.1; NZ_MBLN01000036.1.
DR   AlphaFoldDB; A0A1S1R061; -.
DR   Proteomes; UP000179465; 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          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          190..227
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          80..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  53930 MW;  4E07E378429A3B15 CRC64;
     MARREFRLPD LGEGLAEAEI VHWLVAAGDT VTVNQPLAEV ETAKALVELP SPFAGRLVAT
     HGAEGETILV GTVLVTIEDD EPADADGGGP PAHAPAVGSI GERAGETPAE ATGPPATGSE
     VRDVPARRGG EREPMLVGYG PRASIGAAGL GRARRRGQRA AAPSVPASQA GTPPAPSDPS
     ATVERGHRAL AKPPVRRLAR DLGVDLGRLS GTGPGGSISR ADVETAARGL VTGVPEGTGR
     ESTGRLAEPA AWEPPVPSAL PPAGRPEAAA TGGAGGGQVG RIPAEASFDA ASRTWRVPVS
     GVRRATARAM VSSAFTAPHV TEFLTADLTE TMATRDRIAA LPEFADVKVT PLLFAARALL
     VAVRRHPMIN TSWVEHERRD PEIVVSEAVN LGIAVASPRG LLVPNIPGAD RLDLAGLAHA
     LADLTARTRA GQARPADLTG GTITITNIGV FGVDTGTPVL NPGEAAILAL GAVRPAPWVH
     EGELAVRTVG QLALSFDHRL VDGELGSAVL ADIAAMLTDP ALLLAWS
//
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