ID A0A0F5R256_9BACL Unreviewed; 445 AA.
AC A0A0F5R256;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=VE23_03675 {ECO:0000313|EMBL:KKC46414.1};
OS Paenibacillus sp. D9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=665792 {ECO:0000313|EMBL:KKC46414.1, ECO:0000313|Proteomes:UP000036611};
RN [1] {ECO:0000313|EMBL:KKC46414.1, ECO:0000313|Proteomes:UP000036611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D9 {ECO:0000313|EMBL:KKC46414.1,
RC ECO:0000313|Proteomes:UP000036611};
RA Sharma V., Lin J.;
RT "Genome sequence of surfactant producing, diesel degrading Paenibacillus
RT sp. D9, isolated from diesel contaminated soil.";
RL Submitted (MAR-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:KKC46414.1}.
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DR EMBL; JZEJ01000001; KKC46414.1; -; Genomic_DNA.
DR RefSeq; WP_049867314.1; NZ_JZEJ01000001.1.
DR AlphaFoldDB; A0A0F5R256; -.
DR PATRIC; fig|665792.3.peg.821; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000036611; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase 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}; Hydrolase {ECO:0000313|EMBL:KKC46414.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000036611};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
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 85..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 46799 MW; 8A3B40CC964E3682 CRC64;
MAKFEYRFPE LGEGLHEGEI MTMHIKPGDK VTDDDIIMEV QNDKAVVEVP CPVNGTVLEV
FAKDGQVCHV GEVVAIIDAE GDLPEGAAPA EDSAKEVAKD EAANVAPGAA KADAEVTAKD
AAPAAQPAKA QGAAKGSVLA TPSVRKLARE KGVDITAVQG TGKNGKVTRE DVEQFAAGGG
KSTPAAAPDN AAVAAKGAGE AKAAPVASQG GDRPEERLPF KGIRKIIAGA MAKSAYTAPH
VTLMDEVDVT ALVELRQKAK PVAEKKGVKL TYLPFIVKAL VAACREFPIM NAMLDEESQE
IVLRKYYNIG IATDTDNGLI VPVIEHADRK NVWTIADSIR DLAIRGRDGK LTGAELKGST
ITITNIGSAG GMFFTPIINF PEVAILGVGR ISDKPVIKNG QIVPASVMAL SLSFDHRIID
GATAQNFLNY IKQLLGDPQL LVMEV
//
