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Database: UniProt
Entry: A0A024W1Z5_PLAFA
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ID   A0A024W1Z5_PLAFA        Unreviewed;       408 AA.
AC   A0A024W1Z5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=PFTANZ_04359 {ECO:0000313|EMBL:ETW34924.1};
OS   Plasmodium falciparum Tanzania (2000708).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=1036725 {ECO:0000313|EMBL:ETW34924.1, ECO:0000313|Proteomes:UP000030708};
RN   [1] {ECO:0000313|EMBL:ETW34924.1, ECO:0000313|Proteomes:UP000030708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tanzania (2000708) {ECO:0000313|Proteomes:UP000030708};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Annotation of Plasmodium falciparum Tanzania (2000708).";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETW34924.1, ECO:0000313|Proteomes:UP000030708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tanzania (2000708) {ECO:0000313|Proteomes:UP000030708};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium falciparum Tanzania (2000708).";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = AMP +
CC         diphosphate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier
CC         protein]; Xref=Rhea:RHEA:49288, Rhea:RHEA-COMP:10500, Rhea:RHEA-
CC         COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:83088, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:456215; EC=6.3.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00043803};
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005124}.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00005085}.
CC   -!- SIMILARITY: Belongs to the LplA family.
CC       {ECO:0000256|ARBA:ARBA00008242}.
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DR   EMBL; KI926501; ETW34924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024W1Z5; -.
DR   SMR; A0A024W1Z5; -.
DR   EnsemblProtists; ETW34924; ETW34924; PFTANZ_04359.
DR   eggNOG; KOG3159; Eukaryota.
DR   UniPathway; UPA00537; UER00594.
DR   Proteomes; UP000030708; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd16443; LplA; 1.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR019491; Lipoate_protein_ligase_C.
DR   InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR   PANTHER; PTHR12561; LIPOATE-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12561:SF3; LIPOYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF10437; Lip_prot_lig_C; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF82649; SufE/NifU; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030708}.
FT   DOMAIN          60..242
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   COILED          235..262
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   408 AA;  47943 MW;  1FE5C6DC4E619D27 CRC64;
     MKRIFRLVRR CHYSTEKRTN GPLVLVSNNQ NIHFNLSLEN FLLNNYNDLL KYLNINTIEK
     FNEPILFLWR NNRSIIIGKN QNIWSECNLK NIKEDGVLVA RRFTGGGAVY HDLGNVCFTF
     LNNNINTSSN FLIILNTLKN HFNIEAKTQG RNDITVNDQK CSGSAFKKIK DVFLHHGTIL
     INLEKNILNK YLTPDKIKYI KHGVSSVNAR TINLSEINNN ITCENLCIAL IKEFTKFYEQ
     NYKENINNIK NLENNINNSN FQNKEQININ NTNENNLINN TNIIPNDITV HYIDQNNNIT
     KNPEFLKYYN LLKDWDWCYG KTPKFQNHIW KQFTFGKLEL FFNVSNGFIK DGNIFSDCLD
     INLIDHLKSI FNNDIKYSKE DISIFFKKLN VENKNYLDEV RSWILQEL
//
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