ID A0A0S9DCL6_9MICC Unreviewed; 529 AA.
AC A0A0S9DCL6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-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=ASF21_05125 {ECO:0000313|EMBL:KQO03644.1};
OS Arthrobacter sp. Leaf234.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQO03644.1, ECO:0000313|Proteomes:UP000053418};
RN [1] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Vorholt J.;
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:KQO03644.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMLU01000001; KQO03644.1; -; Genomic_DNA.
DR RefSeq; WP_055767647.1; NZ_LMLU01000001.1.
DR AlphaFoldDB; A0A0S9DCL6; -.
DR STRING; 1736303.ASF21_05125; -.
DR Proteomes; UP000053418; 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 Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 10..85
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 226..263
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 116..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 529 AA; 54678 MW; A9DA8E71A12BA620 CRC64;
MSTPTVAEKL LVFMLPDLGE GLTEAELVSW LVAEGDTVVV DQAIAEVETA KSVVEVPSPF
AGTVAVLHGR PGEVLDVGAP FLSVRPEGAL VSGSGAATPD AAVTSDAAAI DGAAEELRED
SGVPASATRP DERSPVVSEG SGNVLIGYGT PGGLTGGRTR PRKGAVPTGT RPALEGAVDS
TSSPAIASAH LPGQAPAQGP ARTPAGTPAH TPTDPGAAPE RRAPLCVSPL VRKLARDHGV
RLDDVRGSGE KGLILRRDID AAIAAHVSPS DLTDGPDTPA PPAEASVSRD SRSGLAVLER
TPLRGVRRTI ADAMSRSRRE IPEATVWVDV DVTALVELRD GIKRRTPDAV PGILAFVARF
VVAGLARYPA LNSRITTGED GTQELVRVDG VNLGIAAQTD RGLVVPSVRR ADTLSARELD
TEIRRLAALA RTGKATPSDL SSGTFTLNNY GVFGVDGSAA IINYPESAIL GMGRILDRPW
VVDGELAVRK VTELTLAFDH RVCDGGTAGG FLRFVADAME NPGGMLADL
//
