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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//