ID B1HPS1_LYSSC Unreviewed; 444 AA.
AC B1HPS1;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=Bsph_1365 {ECO:0000313|EMBL:ACA38973.1};
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA38973.1, ECO:0000313|Proteomes:UP000002164};
RN [1] {ECO:0000313|EMBL:ACA38973.1, ECO:0000313|Proteomes:UP000002164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41 {ECO:0000313|EMBL:ACA38973.1,
RC ECO:0000313|Proteomes:UP000002164};
RX PubMed=18296527; DOI=10.1128/JB.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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; CP000817; ACA38973.1; -; Genomic_DNA.
DR RefSeq; WP_012293095.1; NC_010382.1.
DR AlphaFoldDB; B1HPS1; -.
DR EnsemblBacteria; ACA38973; ACA38973; Bsph_1365.
DR KEGG; lsp:Bsph_1365; -.
DR HOGENOM; CLU_016733_10_0_9; -.
DR Proteomes; UP000002164; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:ACA38973.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ACA38973.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 139..176
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 89..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 48312 MW; F62BEB29D4280B5F CRC64;
MAFEFRLPDI GEGIHEGEIV KWFVKAGDTV KEDDILCEVQ NDKAVVEIPS PVEGTVEEVL
VGEGTVAVVG DVLIRLDAPG YEDLKLKGDS HAEEKTEAQV QATAESGQNV EKAPAKEEKA
PEKAPEKAET VVDETKRVIA MPSVRKFARD NDVNIREVKG SGKNGRILKE DITNFLNGGG
TVETESATDV TVEEAVQQET TPTAPVVLEG EFPETREKMS GIRKAIAKAM VHSKQTAPHV
TLMDEVDVTA LVAHRKKFKD IAAEKGVKLT YLPYVVKALI STLREFPEFN RSLDDATQEI
IQKHYYNIGI AADTDKGLLV PVIKHADRKS VFAVSNEINE LATKAREGKL APHEMKGASM
SITNIGSAGG QWFTPVINHP EVAILGIGRI SEKPVIKNGE IVAAPVLALS LSFDHRMIDG
ATAQNALNHL KRLLSEPELL LMEA
//
