LIPA_TOXGO
ID LIPA_TOXGO Reviewed; 543 AA.
AC Q86G50;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Lipoyl synthase, apicoplast {ECO:0000255|HAMAP-Rule:MF_03123};
DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_03123};
DE AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_03123};
DE Short=LS {ECO:0000255|HAMAP-Rule:MF_03123};
DE Short=Lip-syn {ECO:0000255|HAMAP-Rule:MF_03123};
DE AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_03123};
DE Flags: Precursor;
GN Name=lipA {ECO:0000255|HAMAP-Rule:MF_03123};
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=RH;
RX PubMed=12860390; DOI=10.1016/s0014-5793(03)00673-2;
RA Thomsen-Zieger N., Schachtner J., Seeber F.;
RT "Apicomplexan parasites contain a single lipoic acid synthase located in
RT the plastid.";
RL FEBS Lett. 547:80-86(2003).
CC -!- FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms
CC into the C-6 and C-8 positions of the octanoyl moiety bound to the
CC lipoyl domains of lipoate-dependent enzymes, thereby converting the
CC octanoylated domains into lipoylated derivatives. {ECO:0000255|HAMAP-
CC Rule:MF_03123, ECO:0000269|PubMed:12860390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[[Fe-S] cluster scaffold protein carrying a second [4Fe-
CC 4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2
CC oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-
CC N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S]
CC cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-
CC methionine + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16585,
CC Rhea:RHEA-COMP:9928, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:14568, Rhea:RHEA-COMP:14569,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:33722, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:78809, ChEBI:CHEBI:83100; EC=2.8.1.8;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03123};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03123};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|HAMAP-Rule:MF_03123};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03123}.
CC -!- SUBCELLULAR LOCATION: Plastid, apicoplast {ECO:0000255|HAMAP-
CC Rule:MF_03123, ECO:0000269|PubMed:12860390}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase
CC family. {ECO:0000255|HAMAP-Rule:MF_03123}.
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DR EMBL; AJ556158; CAD88789.1; -; mRNA.
DR AlphaFoldDB; Q86G50; -.
DR SMR; Q86G50; -.
DR IntAct; Q86G50; 2.
DR MINT; Q86G50; -.
DR VEuPathDB; ToxoDB:TGARI_226400A; -.
DR VEuPathDB; ToxoDB:TGARI_226400B; -.
DR VEuPathDB; ToxoDB:TGCAST_226400; -.
DR VEuPathDB; ToxoDB:TGCOUG_226400; -.
DR VEuPathDB; ToxoDB:TGDOM2_226400; -.
DR VEuPathDB; ToxoDB:TGFOU_226400; -.
DR VEuPathDB; ToxoDB:TGGT1_226400; -.
DR VEuPathDB; ToxoDB:TGMAS_226400; -.
DR VEuPathDB; ToxoDB:TGME49_226400; -.
DR VEuPathDB; ToxoDB:TGP89_226400; -.
DR VEuPathDB; ToxoDB:TGPRC2_226400; -.
DR VEuPathDB; ToxoDB:TGRH88_045960; -.
DR VEuPathDB; ToxoDB:TGRUB_226400; -.
DR VEuPathDB; ToxoDB:TGVAND_226400; -.
DR VEuPathDB; ToxoDB:TGVEG_226400; -.
DR BRENDA; 2.8.1.8; 6411.
DR UniPathway; UPA00538; UER00593.
DR GO; GO:0020011; C:apicoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016992; F:lipoate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102552; F:lipoyl synthase activity (acting on glycine-cleavage complex H protein; IEA:UniProtKB-EC.
DR GO; GO:0102553; F:lipoyl synthase activity (acting on pyruvate dehydrogenase E2 protein); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00206; Lipoyl_synth; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR003698; Lipoyl_synth.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR10949; PTHR10949; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00271; lipoyl_synthase; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00510; lipA; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Apicoplast; Iron; Iron-sulfur; Metal-binding; Plastid;
KW S-adenosyl-L-methionine; Signal; Transferase.
FT SIGNAL 1..63
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123"
FT CHAIN 64..543
FT /note="Lipoyl synthase, apicoplast"
FT /id="PRO_0000398234"
FT DOMAIN 264..482
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 252
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123"
FT BINDING 257
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123"
FT BINDING 278
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123"
FT BINDING 282
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123"
FT BINDING 285
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123"
FT BINDING 493
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123"
SQ SEQUENCE 543 AA; 58706 MW; 1DDCD0A1150680E6 CRC64;
MAYFFDFPTD TWVEDASPGG PPKRAFGHGL AAGSSHFASP VSRRRLPTIT ALLLFSLLSA
SQSGALSVSQ CSRRVSLGPL LSRVSSVSCT PSAAASALAS SLYPTDSLSS VEGSVAPRPP
PSSLAFVLRR VPPAAYSSSL SPSVLRFKHS LPRPLQGSLV CAPGILGGAA GSARFAGCCG
SQGRSCGSGK NPELPLKGSK DEVIPRVGTS TAGPRPDWFH VPAPQAASRG AEESRYQQLQ
KQIRGLDLHT VCEEAKCPNI GECWNGGTAT LILLGDTCTR GCRFCAIKTS SKPPPPDPLE
PEKVADAVAK WDIDYVVMTS VDRDDMPDGG AGHFARTVQL VKKAKPSMLI ECLVSDFQGM
EESVRTLAQS GLDVYAHNIE TVRRLTPYVR DKRAKYDQSL RVLHLAKQFN PSLFTKSSIM
LGLGETSEEV VRTLRDLRDH DVDVVTLGQY LRPTKQQLGV VEYVTPETFK KYQDIAEEMG
FKYVASGPLV RSSYKAGEYY MKHLIDDARK HGRRETVKQV KLEADVGTLK GTTTTFQVNE
KEA
