ID A0A0L0BG09_9MICC Unreviewed; 518 AA.
AC A0A0L0BG09;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AC792_08900 {ECO:0000313|EMBL:KNC19025.1};
OS Arthrobacter sp. RIT-PI-e.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1681197 {ECO:0000313|EMBL:KNC19025.1, ECO:0000313|Proteomes:UP000053253};
RN [1] {ECO:0000313|Proteomes:UP000053253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-e {ECO:0000313|Proteomes:UP000053253};
RA Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-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:KNC19025.1}.
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DR EMBL; LGIU01000062; KNC19025.1; -; Genomic_DNA.
DR RefSeq; WP_049830193.1; NZ_LGIU01000062.1.
DR AlphaFoldDB; A0A0L0BG09; -.
DR STRING; 1681197.AC792_08900; -.
DR PATRIC; fig|1681197.3.peg.1161; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000053253; 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:UP000053253};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 21..96
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 215..252
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 53464 MW; D0E25C60C3135B53 CRC64;
MPADPHTTDE APGDPAASGR VREFRLPDLG EGLTESEILR WHVAEGEVVE LNQVIADVET
AKAVVELPSP CAGVVLRLLE GAGTVVEVGT PIISFTLPVP GASPGAPQGP TAVAGGEPGT
PDAGGAPRRR EPTLVGYGAT PEQEGRPRRR SRSVGRACPG SAPQLPEPEG PPLAERRAPL
SGPRARPTPD VPPAAGPPAP PVTGSAVPHP AERPRSTPPV RKLARDLGIA LDTLTGSGPG
ALITREDVLA ALTQPPTPRE ADGPRHVDPA GPGTPREAPA GRATPPGEAR LPIRGIRKLT
AAAMVSSAFT APHATEFLTI DVTPTLELLE EVRRNPASTG TRITMLSVVA KAVCIAAARN
PSLNSSWDER AQEIVQYAGV NLGIAAATPR GLVVPNIKGA ERLTLLELAR ALAALTETAR
SGRTTPAALA GGTLSITNIG VFGIDAGTPI LTPGEAAILA VGAVRRMPWE YRDAVALRSV
LTLSLSFDHR LVDGEQGSHF LADVGTILSR PAMVLAMV
//
