ID S6BEI8_BABBO Unreviewed; 417 AA.
AC S6BEI8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=BBOV_II001300 {ECO:0000313|EMBL:BAN64519.1};
OS Babesia bovis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5865 {ECO:0000313|EMBL:BAN64519.1};
RN [1] {ECO:0000313|EMBL:BAN64519.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Texas {ECO:0000313|EMBL:BAN64519.1};
RX PubMed=25124460; DOI=10.1186/1471-2164-15-678;
RA Yamagishi J., Wakaguri H., Yokoyama N., Yamashita R., Suzuki Y., Xuan X.,
RA Igarashi I.;
RT "The Babesia bovis gene and promoter model: an update from full-length EST
RT analysis.";
RL BMC Genomics 15:678-678(2014).
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; AK440725; BAN64519.1; -; mRNA.
DR AlphaFoldDB; S6BEI8; -.
DR VEuPathDB; PiroplasmaDB:BBOV_II001300; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:RHEA.
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 2: Evidence at transcript level;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:BAN64519.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:BAN64519.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 31..106
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 143..180
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 417 AA; 45278 MW; 4E53C564D392787C CRC64;
MLASLFQFGS RSVSRLAYAR HFHRSVQRNK LTTFHLSDIG EGISEVELVR WNKNVGDEVE
EMETVCTVQS DKAAVDITSR YTGLVKKLYV EQGKLIKIGS PLMDIDAEDD TPAVSEPTET
TKSSIPSKPV AQSFKRSHDD SVRAAPSVRQ LAKQLGVDIT KVVPSGSNSQ ITREDVEKFA
ASSQSVSGGV PGDFVKLNSV GRGMVKSMVA SLEVPHVTVG EDVDLTELKS YYLQKRALET
DIKLTMTPFL LKAFSLALSE NPIMNSKFKG DGYIAYKEHN INVAVATDHG LLVPVIRNVE
SKSIRALQVD LARVQRLAAE MRLSPGDMSG GTATLSNLGA IGGTHVNARL FDGQGTIVAF
GAARKTPCYV GDELVPRDIA CLGVTADHRH IDGAAIARFA AALKRYLQDV SNFDVHY
//
