ID   C1D0B4_DEIDV            Unreviewed;       504 AA.
AC   C1D0B4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=Deide_23470 {ECO:0000313|EMBL:ACO47383.1};
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47383.1, ECO:0000313|Proteomes:UP000002208};
RN   [1] {ECO:0000313|EMBL:ACO47383.1, ECO:0000313|Proteomes:UP000002208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC   {ECO:0000313|Proteomes:UP000002208};
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO47383.1; -; Genomic_DNA.
DR   RefSeq; WP_012694504.1; NC_012526.1.
DR   AlphaFoldDB; C1D0B4; -.
DR   STRING; 546414.Deide_23470; -.
DR   PaxDb; 546414-Deide_23470; -.
DR   KEGG; ddr:Deide_23470; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_0; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000002208; 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:UP000002208};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ACO47383.1}.
FT   DOMAIN          1..76
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          79..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   504 AA;  53698 MW;  7FA3AC5BFE2B340F CRC64;
     MKEVLLPELA ESVVEGEILK WLVQEGDTIA LEQPLCEVMT DKVTVELPSP VAGVLRQRLA
     NEGDVVAVHA AIALIDETGG GASSSAPSAM QAIQDTAESP ATADAQLPPQ AQEEREQIGG
     SIVEASHLPK ADDDSSSLFK AFASDEQVKV QGLGGRTPAP QGAAQPVRND GRVLAVPAAR
     QLARELGLDL NRIQGSGPNG RIRVSDVLAQ TQGQTASSTA ASSMPASAPA PQPASTAQAA
     AQPAPASSKA AQGGLPVAPV QYRTPKGYEH LEDRVPLRGM RRAISNQMVA SHLYTVRTLT
     VDEVNLTRLV EFRNRVKDEA KAADVKLSYL PFIFKAVAVA LRKYPSLNTS FDEATQEIVQ
     KRYYNMGMAV ATDAGLTVPV LKDVGRKSVF ELAREVVDLA GRAQAGKLQP DELAGSTFSI
     TNIGSIGALF SFPIINVPDA AILGVHSIVK RPIVDEDDNI VVAHMMYLSL SFDHRLVDGA
     EAARFCKEVI RLLENPDRLM LEAM
//