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Database: UniProt
Entry: Q5VGY2_PLAFA
LinkDB: Q5VGY2_PLAFA
Original site: Q5VGY2_PLAFA 
ID   Q5VGY2_PLAFA            Unreviewed;       640 AA.
AC   Q5VGY2;
DT   07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   07-DEC-2004, sequence version 1.
DT   22-FEB-2023, entry version 87.
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=dlat {ECO:0000313|EMBL:AAS49638.1};
OS   Plasmodium falciparum (malaria parasite P. falciparum).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5833 {ECO:0000313|EMBL:AAS49638.1};
RN   [1] {ECO:0000313|EMBL:AAS49638.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=D10 {ECO:0000313|EMBL:AAS49638.1};
RX   PubMed=15612915; DOI=10.1111/j.1365-2958.2004.04407.x;
RA   Foth B.J., Stimmler L.M., Handman E., Crabb B.S., Hodder A.N.,
RA   McFadden G.I.;
RT   "The malaria parasite Plasmodium falciparum has only one pyruvate
RT   dehydrogenase complex, which is located in the apicoplast.";
RL   Mol. Microbiol. 55:39-53(2005).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={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; AY484443; AAS49638.1; -; mRNA.
DR   AlphaFoldDB; Q5VGY2; -.
DR   SMR; Q5VGY2; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1020800; -.
DR   VEuPathDB; PlasmoDB:Pf7G8-2_000306400; -.
DR   VEuPathDB; PlasmoDB:Pf7G8_100025300; -.
DR   VEuPathDB; PlasmoDB:PfCD01_100026100; -.
DR   VEuPathDB; PlasmoDB:PfDd2_100026200; -.
DR   VEuPathDB; PlasmoDB:PfGA01_100026200; -.
DR   VEuPathDB; PlasmoDB:PfGB4_100025900; -.
DR   VEuPathDB; PlasmoDB:PfGN01_100026400; -.
DR   VEuPathDB; PlasmoDB:PfHB3_100025300; -.
DR   VEuPathDB; PlasmoDB:PfIT_100024900; -.
DR   VEuPathDB; PlasmoDB:PfKE01_100026200; -.
DR   VEuPathDB; PlasmoDB:PfKH01_100025400; -.
DR   VEuPathDB; PlasmoDB:PfKH02_100026300; -.
DR   VEuPathDB; PlasmoDB:PfML01_100025100; -.
DR   VEuPathDB; PlasmoDB:PfNF135_100026100; -.
DR   VEuPathDB; PlasmoDB:PfNF166_100025700; -.
DR   VEuPathDB; PlasmoDB:PfNF54_100025900; -.
DR   VEuPathDB; PlasmoDB:PfSD01_100025500; -.
DR   VEuPathDB; PlasmoDB:PfSN01_100026300; -.
DR   VEuPathDB; PlasmoDB:PfTG01_100026200; -.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   CDD; cd06849; lipoyl_domain; 2.
DR   Gene3D; 2.40.50.100; -; 2.
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; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF75; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT 5 OF PYRUVATE DEHYDROGENASE COMPLEX, CHLOROPLASTIC; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   2: Evidence at transcript level;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AAS49638.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AAS49638.1};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..640
FT                   /note="Dihydrolipoamide acetyltransferase component of
FT                   pyruvate dehydrogenase complex"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004263038"
FT   DOMAIN          52..127
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          182..257
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   640 AA;  73890 MW;  185718D379E16CBC CRC64;
     MLYNLIILIF YLRFSKCISK NNNYGYINFG TFSNVVNNSN NLRNRKNVVF SKIEIKMPAL
     SSTMTTGKIV KWNKNIGDYV NLGDIIMTVE SDKADMDVEA FDEGFLRVKR LEDGCEANVG
     DVLGVLTTEE NENMDEKKYN DGDINKTENE IKVLNPDKDK SEQIIKEDIH FVKKHINDDV
     NEEKIFIPFI KCKKKKAKIN KWLKNENDFV KKNDLLLYVE DDKSTIEVES PYSGIIKKLL
     VKEGQFVDLD KEVAIISITE EKDNEKEKIE EPFKNKEDEE INRDNILIHY INKIKKSEEG
     RKFLKNLSEQ EEKTLEERLK LNYEKYNKIS NDLFRSSEST KDYVLKEKEN ESQYEMVLPS
     ASELMRQNKL NPKDITNRKT PNRITYEDVD AFLNGHKNNS TNVTYCEKPK VETIEYGDPK
     TVDMTNIQKS IKNNMMLTLT VPVFRVTHLI KTNELLKLYE KVKQKISMSV IINKCVSSVL
     LNHPLIYSTY IDKDNGKILY NKDVNIGNAL GLPDSLLTPV LKKVDKKDIY TLANEWKILV
     EKGKNGLLSS NDMTGSNFYI SNLGMFNTYQ FDAILPKNSS CILSIGTNIG SIDNLEDLKI
     QKGMMMTLTC DHRHIYGSHA AAFMNDLSKF IEKDIMKIFL
//
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