GenomeNet

Database: UniProt
Entry: W7A6S6_9APIC
LinkDB: W7A6S6_9APIC
Original site: W7A6S6_9APIC 
ID   W7A6S6_9APIC            Unreviewed;       423 AA.
AC   W7A6S6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=C922_00520 {ECO:0000313|EMBL:EUD68832.1};
OS   Plasmodium inui San Antonio 1.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD68832.1, ECO:0000313|Proteomes:UP000030640};
RN   [1] {ECO:0000313|EMBL:EUD68832.1, ECO:0000313|Proteomes:UP000030640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD68832.1,
RC   ECO:0000313|Proteomes:UP000030640};
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 inui San Antonio 1.";
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}.
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; KI965461; EUD68832.1; -; Genomic_DNA.
DR   RefSeq; XP_008814358.1; XM_008816136.1.
DR   AlphaFoldDB; W7A6S6; -.
DR   EnsemblProtists; EUD68832; EUD68832; C922_00520.
DR   GeneID; 20035794; -.
DR   VEuPathDB; PlasmoDB:C922_00520; -.
DR   OrthoDB; 168805at2759; -.
DR   UniPathway; UPA00537; UER00594.
DR   Proteomes; UP000030640; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EUD68832.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          61..243
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   423 AA;  48693 MW;  11082A89BFA78F37 CRC64;
     MKQRMNVALK RWYSSERTKS ANPLILISNN QNIHFNLSLE NFLLNNYSDL LKYLNVNTIE
     KYDDPVLFLW RNNRSIIIGK NQNIWSECNL ENIKKDNVQV ARRFTGGGAV YHDLENVCFT
     FLNNTLNTDN NFSIILKTLK RHFSIDAKKQ GRNDITVNDR KCSGSAFKKV RNVFLHHGTI
     MVNLEKDVLK MYLTPDKMKY IKHGVSSVNA RTINLKEINQ NITCQNLCCA LIKEFEAFYK
     KGVSDTEGEG SNAATLHVED YTCGDSGATS LGQPNGHLTA NLNKREKSTD NLVDISSPIS
     NHFNIHYIDT NESITKNPEF LKYLNLLKDW DWCYGKTPKF QNRLCRQFNF GKLEIFFNVS
     DGMIKDGNIF SDCLDVNLVE QLKFIFNNDV KYSKDSVSSF LRGLKVENKD PLAEVTEWIL
     QEL
//
DBGET integrated database retrieval system