ID A7AWP7_BABBO Unreviewed; 374 AA.
AC A7AWP7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=BBOV_I003930 {ECO:0000313|EMBL:EDO05475.1};
OS Babesia bovis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5865 {ECO:0000313|EMBL:EDO05475.1, ECO:0000313|Proteomes:UP000002173};
RN [1] {ECO:0000313|EMBL:EDO05475.1, ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2Bo {ECO:0000313|EMBL:EDO05475.1};
RX PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA Nene V.M.;
RT "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT hemoprotozoa.";
RL PLoS Pathog. 3:1401-1413(2007).
RN [2] {ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33294524; DOI=10.1016/j.dib.2020.106533;
RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT "Transcriptome dataset of Babesia bovis life stages within vertebrate and
RT invertebrate hosts.";
RL Data Brief 33:106533-106533(2020).
RN [3] {ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33069745;
RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT "Comparative analysis of gene expression between Babesia bovis blood stages
RT and kinetes allowed by improved genome annotation.";
RL Int. J. Parasitol. 51:123-136(2021).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDO05475.1}.
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DR EMBL; AAXT01000005; EDO05475.1; -; Genomic_DNA.
DR RefSeq; XP_001609043.1; XM_001608993.1.
DR AlphaFoldDB; A7AWP7; -.
DR STRING; 5865.A7AWP7; -.
DR EnsemblProtists; EDO05475; EDO05475; BBOV_I003930.
DR GeneID; 5477259; -.
DR KEGG; bbo:BBOV_I003930; -.
DR VEuPathDB; PiroplasmaDB:BBOV_I003930; -.
DR eggNOG; KOG3159; Eukaryota.
DR InParanoid; A7AWP7; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000002173; 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 NCBIfam; TIGR00545; lipoyltrans; 1.
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:EDO05475.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002173}.
FT DOMAIN 55..239
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 374 AA; 42464 MW; DB2E1FE609B07436 CRC64;
MVLFSNLCRR FSTKIKTGNR SVKVLISSEN DIYFNLALEN ALLKSYGKNM AIDNKYEVPI
LFLWRNSPCV IVGCNQNVWS ECNLDNVRKD GVNLVRRFTG GGAVYQDLGN TCFTFISSPK
DYSFERNCNL ICSAVTKLIG EKCEPSGRND LCVNGLKFSG SAFKLLPNAA LHHGTLLINI
NQGSLDKYLT PDISKLEKHN VKSVKARVTN LCQFNETVTH EMICNAIIDE VASFYKSPTT
NVEYIDAKAK CCNDEAFQEC YHKLKDTKWI YGEEMKRFKS LKQRFDFGSI EICFDIQDGN
VVKFWVYSDS LETDFITWLQ LKLNQTAINV PYEELGETLK HLEYEASNDV LVAVKKWLIS
SLSNEVDGTI KNNV
//
