ID A0A182W7H1_9DIPT Unreviewed; 541 AA.
AC A0A182W7H1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=dihydrolipoyllysine-residue acetyltransferase {ECO:0000256|ARBA:ARBA00013114};
DE EC=2.3.1.12 {ECO:0000256|ARBA:ARBA00013114};
DE AltName: Full=Pyruvate dehydrogenase complex component E2 {ECO:0000256|ARBA:ARBA00032943};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN006293-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN006293-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN006293-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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DR AlphaFoldDB; A0A182W7H1; -.
DR STRING; 112268.A0A182W7H1; -.
DR EnsemblMetazoa; AMIN006293-RA; AMIN006293-PA; AMIN006293.
DR VEuPathDB; VectorBase:AMIN006293; -.
DR OrthoDB; 5483022at2759; -.
DR Proteomes; UP000075920; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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 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; IPR045257; E2/Pdx1.
DR InterPro; IPR006257; LAT1.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01349; PDHac_trf_mito; 1.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 76..152
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 169..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 57702 MW; 62DF93484FA9FC1E CRC64;
MLRTIIVRNE NLLLQGSIRK LLKGTAVRSL SSECAKRSAA GHRRNSHNLS NGHNNLKTVT
WRTTLVRGYC SGFPAHSKVL LPALSPTMEL GTIVSWEKKE GDKLNEGDLL AEIETDKATM
GFETPEEGYL AKILVQAGQK DVPIGKLVCI IVENESDVAA FKDYKDTGAA PAKPAAAPAP
PAPAAAPPAP TPPPVAAPPP PPPVAASPQP MTAVEQRGPR VYASPMAKKL AEQQRLRLEG
KGSGLFGSLT SKDLAGMQAD GAAPSAGAPA AAPSIPAGAA YVDIPVSNIR GVIAKRLLES
KTTIPHYYLT VDVNMDQVSK LRARFNKQLE KEGVKLSIND FIIKAAAMAC KKVPEANSAW
MNTVIRQFDA VDVSVAVSTD RGLITPIVFS ADRKGIADIS KDVKNLAAKA REGKLQPQEF
QGGTFSVSNL GMFGVTHFCA IINPPQSCIL AVGGTQKRLV PDKDSEAGFK ESDYVAVTLS
CDHRTVDGAV GARWLQYFRQ FLEDPNSMLL SAGIKRNESP SQEGVLAEQN MGDKGKSRNT
N
//