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Database: UniProt
Entry: A0A433HS58_9BACI
LinkDB: A0A433HS58_9BACI
Original site: A0A433HS58_9BACI 
ID   A0A433HS58_9BACI        Unreviewed;       408 AA.
AC   A0A433HS58;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=ELQ35_05860 {ECO:0000313|EMBL:RUQ31102.1};
OS   Peribacillus cavernae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=1674310 {ECO:0000313|EMBL:RUQ31102.1, ECO:0000313|Proteomes:UP000267430};
RN   [1] {ECO:0000313|EMBL:RUQ31102.1, ECO:0000313|Proteomes:UP000267430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L5 {ECO:0000313|EMBL:RUQ31102.1,
RC   ECO:0000313|Proteomes:UP000267430};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT   sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT   Center where the Viking Spacecraft were Assembled.";
RL   Submitted (DEC-2018) 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:RUQ31102.1}.
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DR   EMBL; RYZZ01000006; RUQ31102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433HS58; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000267430; 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|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267430};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          115..152
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   408 AA;  44987 MW;  0085C03C739F1F29 CRC64;
     MSYMFILPDI GEGLHEAEIV TWFVKTGDFV KENQNIVEVQ TDKAVVELPS PYTGIVESLG
     AEEGEIVKVG EPLIRFQIEN GSNSKASCGQ EKEDLHFENS VSSIHTSAKV SNRVIAAPGV
     RKLARTLGVD LINVTPSAKG GRVTAGDVTA FKERLDQTNE AVSTIEKPVD KRLPIEFPET
     EKRVRIKGIR KKIFENMKRS QLAAAQCTGM EEINVTRLVE ARKRILPYAE KKGIKMTYLP
     FIIKAVAKTL TQIPVFNSSV DEENMEIIYH PSIHIGIATA TQAGLIVPVL KNADQKSIFE
     MAMELERLTN KAHSKQLTAE ELTGSTFTIS NTGSKGGFFA TPIINYPEAA ILGVHSIKKK
     PVVEDDQIII GEMMGMSLTF DHRIIDGEPA GIFISTFAEY LQVPELLM
//
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