LIAS_VITVI
ID LIAS_VITVI Reviewed; 393 AA.
AC A5CB81;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Lipoyl synthase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03128};
DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_03128};
DE AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_03128};
DE Short=LS {ECO:0000255|HAMAP-Rule:MF_03128};
DE Short=Lip-syn {ECO:0000255|HAMAP-Rule:MF_03128};
DE AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_03128};
GN Name=LIP1 {ECO:0000255|HAMAP-Rule:MF_03128}; ORFNames=VITISV_021769;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir;
RX DOI=10.1371/journal.pone.0001326;
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "A high quality draft consensus sequence of the genome of a heterozygous
RT grapevine variety.";
RL PLoS ONE 2:E1326-E1326(2007).
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_03128}.
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_03128};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03128};
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_03128};
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_03128}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03128}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03128}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase
CC family. {ECO:0000255|HAMAP-Rule:MF_03128}.
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DR EMBL; AM488835; CAN73265.1; -; Genomic_DNA.
DR RefSeq; XP_002266132.2; XM_002266096.4.
DR AlphaFoldDB; A5CB81; -.
DR SMR; A5CB81; -.
DR STRING; 29760.VIT_00s0445g00020.t01; -.
DR PRIDE; A5CB81; -.
DR GeneID; 100251365; -.
DR KEGG; vvi:100251365; -.
DR eggNOG; KOG2672; Eukaryota.
DR OrthoDB; 610833at2759; -.
DR UniPathway; UPA00538; UER00593.
DR ExpressionAtlas; A5CB81; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; 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 HAMAP; MF_03128; Lipoyl_synth_plantM; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR031691; LIAS_N.
DR InterPro; IPR003698; Lipoyl_synth.
DR InterPro; IPR027527; Lipoyl_synth_mt.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR10949; PTHR10949; 1.
DR Pfam; PF16881; LIAS_N; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00271; lipoyl_synthase; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00510; lipA; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..393
FT /note="Lipoyl synthase, mitochondrial"
FT /id="PRO_0000398857"
FT DOMAIN 131..351
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03128"
FT BINDING 120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03128"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03128"
FT BINDING 146
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_03128"
FT BINDING 150
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_03128"
FT BINDING 153
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_03128"
FT BINDING 362
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03128"
SQ SEQUENCE 393 AA; 43477 MW; 18F30ED79ECD49A3 CRC64;
MYTRLSSLAL RHHRHNHNNS VLLLSSLISL RHCSSPPTNP EPPQTLASLR HRLAVESPSL
SDFVRLQTSD DYSVEVGTKK KPLSKPKWMK ESIPGGAKYT QIKKKLRQLN LHTVCEEARC
PNMGECWSGG ETGTATATIM ILGDTCTRGC RFCNVKTSRT PPPPDPDEPS KVAEAIASWG
LDYVVITSVD RDDLPDQGSG HFAETVQKLK ILKPNMLIEA LVPDFRGDPG CVEKVSKSGL
DVFAHNIETV EELQSAVRDH RANFKQSLEV LKLAKEYADA GTLTKTSIML GCGETPDQVV
RTMEKVRAAG VDVMTFGQYM RPSKRHMPVS EYITPEAFEK YRILGMDMGF RYVASGPMVR
SSYKAGEFYI KSMIDADRAM SWASSSPSPL PAA
