ID A1RBF6_PAEAT Unreviewed; 521 AA.
AC A1RBF6;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 113.
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=AAur_3891 {ECO:0000313|EMBL:ABM08106.1};
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Paenarthrobacter.
OX NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM08106.1, ECO:0000313|Proteomes:UP000000637};
RN [1] {ECO:0000313|EMBL:ABM08106.1, ECO:0000313|Proteomes:UP000000637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1 {ECO:0000313|EMBL:ABM08106.1,
RC ECO:0000313|Proteomes:UP000000637};
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.,
RA Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
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; CP000474; ABM08106.1; -; Genomic_DNA.
DR RefSeq; WP_011776493.1; NC_008711.1.
DR AlphaFoldDB; A1RBF6; -.
DR STRING; 290340.AAur_3891; -.
DR KEGG; aau:AAur_3891; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_11; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000000637; 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; 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 ECO:0000313|EMBL:ABM08106.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:ABM08106.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ABM08106.1}.
FT DOMAIN 3..79
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 108..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 54519 MW; 7D2832BA48951DCC CRC64;
MTVKKFNLPD VGEGLTEAEV VAWKVKPGDV VAINDVLCEI ETAKSLVELP SPFAGTVTEL
LVEEGITVEV GTAIIAVSEG QDGDAAPVTP VAPEAPAVEM PLYGKLLVDD EGDDNRPAGG
PLVGSGPKAD AVKRRARKRP AGPVVEAATV EENAEGTVQD HQAALEAKAA ETPAAHRTTA
AAAGVAPVTQ TPAAQAQPVT AEAPQAAASR GAAISGTISG LVNKVLAKPP VRKFARDLGI
DLADVVATGQ RGEVTREDLV SYQAQRDAEH DQADSFWGAS KKPQDQRVER MPVKGVRKAT
AKAMVDSAFS APHVSIFVDV DASRTMEFVK RLKVSRDFEG IKVSPLLILA KAVIWAAARN
PSVNATWVDN ADGKGGAEIH VKHYMNLGIA AATPRGLMVP NIKDAQDLSL KELALALNEL
ATKARAGKTQ PAEMQGGSLT VTNIGALGID TGTPIINPGE VAIIAFGTIK QKPWVLDGEV
IPRWITTLGG SFDHRVVDGD LSARFMADVA SILEEPALLL D
//