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Database: UniProt/TrEMBL
Entry: A0A089LTP4_9BACL
LinkDB: A0A089LTP4_9BACL
Original site: A0A089LTP4_9BACL 
ID   A0A089LTP4_9BACL        Unreviewed;       439 AA.
AC   A0A089LTP4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=PSTEL_15560 {ECO:0000313|EMBL:AIQ64292.1};
OS   Paenibacillus stellifer.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ64292.1, ECO:0000313|Proteomes:UP000029507};
RN   [1] {ECO:0000313|EMBL:AIQ64292.1, ECO:0000313|Proteomes:UP000029507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ64292.1,
RC   ECO:0000313|Proteomes:UP000029507};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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}.
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DR   EMBL; CP009286; AIQ64292.1; -; Genomic_DNA.
DR   RefSeq; WP_038696452.1; NZ_CP009286.1.
DR   AlphaFoldDB; A0A089LTP4; -.
DR   STRING; 169760.PSTEL_15560; -.
DR   KEGG; pste:PSTEL_15560; -.
DR   HOGENOM; CLU_016733_10_0_9; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000029507; Chromosome.
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:AIQ64292.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029507};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          1..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          134..171
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          79..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  46307 MW;  0880E49E70ECBE50 CRC64;
     MTKFNYPFPE LGEGLHEGEI IKMHIKAGDK VTDEDIIMEV QNDKAVVEVP CPVNGTVLEV
     LAKDGDVFRV GQTVAVIDAE GDIPEQEGGH EEEQGAQEAD SAKGSADTAS SPAATSPSDA
     KAGEAVPAPD RDVLATPGVR KFARDNSVDI SKVNGTGKSG KITREDVEAF LNGGQSAAPA
     SASAAAEGAP ADKTAAPAAA ASGNVSLEEE RVPFKGIRKA IANAMVKSAY TAPHVTIMDE
     VDVTELVAFR TRMKPVAEKK GVKVTYLPFI VKALVAASRQ FPALNATIDE EANEIVYKKY
     YNIGIATDTD NGLIVPVIKD ADRKSIWMIA SAISDLAARG REGKLSPNEM KGSTISITNI
     GSAGGMFFTP IINYPEVAIL GTGRISEKPV VKNGEIVAAP VMALSLSFDH RLIDGATAQN
     FMNYIKSLLA NPELLVMEV
//
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