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Database: UniProt
Entry: A0A0Q8UXF7_9MICO
LinkDB: A0A0Q8UXF7_9MICO
Original site: A0A0Q8UXF7_9MICO 
ID   A0A0Q8UXF7_9MICO        Unreviewed;       432 AA.
AC   A0A0Q8UXF7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=ASE16_11975 {ECO:0000313|EMBL:KRC49946.1};
OS   Leifsonia sp. Root227.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC49946.1, ECO:0000313|Proteomes:UP000051819};
RN   [1] {ECO:0000313|EMBL:KRC49946.1, ECO:0000313|Proteomes:UP000051819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root227 {ECO:0000313|EMBL:KRC49946.1,
RC   ECO:0000313|Proteomes:UP000051819};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC49946.1, ECO:0000313|Proteomes:UP000051819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root227 {ECO:0000313|EMBL:KRC49946.1,
RC   ECO:0000313|Proteomes:UP000051819};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KRC49946.1}.
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DR   EMBL; LMIO01000003; KRC49946.1; -; Genomic_DNA.
DR   RefSeq; WP_055896432.1; NZ_LMIO01000003.1.
DR   AlphaFoldDB; A0A0Q8UXF7; -.
DR   STRING; 1736496.ASE16_11975; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000051819; 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:UP000051819};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          146..183
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          79..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  45695 MW;  B3B2AB720FD5BC9A CRC64;
     MSAQVFRLPD LGEGLTEAEL VRWLVAVGDV IAVDQPIAEV ETAKSVVEVP SPFAGAVSAL
     HGEEGEALAV GAPLIEVDEP QSTQDKPQSA PENQRTPDQT STGGSGHVLV GYGTTELHRS
     GRRRVRRSTV TATAVSVPAR SGSVPVISPV VRTLARTHGI DLSTVRATGE GGVITRRDVE
     EAFAAAAPAA EPTVDQRTGL ALRASTPFSL FRRTVAANMT RSRSEIPEAT VWVDVDVTEL
     WDARRRLRFG DRTPSLLSFV ARFTLAALAR RPELAGRVTA DGAGIDTFDG VNLGFAVDSP
     RGLVVPVVRR ADRMTIRELD GAFDRLTRDA RAGGLAPAEL TGSTFTINNY GSLGVDGSAA
     IINHPEVAIL GIGRMIERPW VVDGAIVPRR IAQLSLVFDH RVTDGGVAAG LLRDIADAME
     SPLALLADAP PV
//
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