ID Q4U9K9_THEAN Unreviewed; 422 AA.
AC Q4U9K9;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=TA08530 {ECO:0000313|EMBL:CAI76494.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI76494.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI76494.1, ECO:0000313|Proteomes:UP000001950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
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; CR940353; CAI76494.1; -; Genomic_DNA.
DR RefSeq; XP_953119.1; XM_948026.1.
DR AlphaFoldDB; Q4U9K9; -.
DR STRING; 5874.Q4U9K9; -.
DR GeneID; 3863119; -.
DR KEGG; tan:TA08530; -.
DR VEuPathDB; PiroplasmaDB:TA08530; -.
DR eggNOG; KOG0558; Eukaryota.
DR InParanoid; Q4U9K9; -.
DR OMA; MPFCIKA; -.
DR OrthoDB; 1399at2759; -.
DR Proteomes; UP000001950; Chromosome 4.
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 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; 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 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 Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000001950};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 41..116
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 117..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 46637 MW; D1C07D688BA4B593 CRC64;
MMRLLNLYRL CSPCFSRPKT PCIINNFSSR FLHLSSKNLA LTTFKLSDIG EGINEVQLVK
WEKSVGDEVE EMESVCTVQS DKAAVEITSR YTGIVKKLYV NEGDTVKIGS PLMDIDTVDE
VPDDTPNNNS SSNLNDPKRH YSTIPESKFF LNSLGTAKKS FSTSSTTQDD VEEVKVDFIG
EAMVKSMVAS LEVPHVTVGE ECDVTSLIQL YKSYRNVPAE GSDQESQPKI TITPFIIKSI
SLALEKVPII NSKFNTANAG KGPSSYFLYK NHNISVAINT KNGLMVPNIK NVNKLTIREI
QRELSSLQQK ANSKTLNFND IKGGTCALSN LGSLGGTFVK ARLFDGQAAI IAFGRSIQRV
VPVPKTLKTV STNLDDYTLE CRSICNIGVT ADHRHIDGAI ITSFISHLKH FLENADSLRQ
YY
//
