ID A0A0V0WJW7_9BILA Unreviewed; 457 AA.
AC A0A0V0WJW7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
DE Flags: Fragment;
GN Name=ZK669.4 {ECO:0000313|EMBL:KRX75994.1};
GN ORFNames=T06_8677 {ECO:0000313|EMBL:KRX75994.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX75994.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX75994.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX75994.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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:KRX75994.1}.
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DR EMBL; JYDK01000110; KRX75994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WJW7; -.
DR STRING; 92179.A0A0V0WJW7; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:KRX75994.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KRX75994.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 46..120
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 160..197
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 120..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX75994.1"
FT NON_TER 457
FT /evidence="ECO:0000313|EMBL:KRX75994.1"
SQ SEQUENCE 457 AA; 51001 MW; 10B29B8A51647EDA CRC64;
LENLFTQKMF HRLLLSRKVL LWEISKIPWN VCKHHFHHCQ ILGGRLMQIR LSDIGEGIAE
VQMKQHVKIG DQIQEFENLC DVQSDKASVT ITSRFSGTVR RLYCEIDEIV PVGSPLLDIE
TEDGSENIPP DKAADQSEDI PKRPASDDSF TISKNKKTVI TTPSVRRLAM ENKINLSEIK
GTGPGGRILK EDLLNVISAE IDANVDASED EKKSLSTTSA LIEDQVIPIR GYRRAMFVFQ
ACIIHSNRII MLLLLKVNAD ALIKLRHSLM SMNELEKVKI TYLSIQIKAL SLALLRFPML
NAHLNDTVTE LICKTSHNIS FAVDTPDGLV VPFISDCQKK SIIEIAKQIS HLQAKALNNK
LTNAELVGGT FTMSNIGSIG GTYASPVIFP PQVAICAVGR FQKLPRYDEQ SNLKMCNIMP
VSWAADHRII DGAMVAKFSN LFKVYLENPS LMLAELN
//
