(data stored in SCRATCH zone)

SWISSPROT: LIPA_PENRW

ID   LIPA_PENRW              Reviewed;         416 AA.
AC   B6HFQ1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Lipoyl synthase, mitochondrial {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   ORFNames=Pc20g03200;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Catalyzes the radical-mediated insertion of two sulfur
CC       atoms into the C-6 and C-8 positions of the octanoyl moiety bound
CC       to the lipoyl domains of lipoate-dependent enzymes, thereby
CC       converting the octanoylated domains into lipoylated derivatives.
CC       {ECO:0000255|HAMAP-Rule:MF_03123}.
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 =
CC         (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine +
CC         [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen
CC         sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:16585, Rhea:RHEA-COMP:9928, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:14568, Rhea:RHEA-COMP:14569, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:29034, ChEBI:CHEBI:29919,
CC         ChEBI:CHEBI:33722, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:78809,
CC         ChEBI:CHEBI:83100; EC=2.8.1.8; Evidence={ECO:0000255|HAMAP-
CC         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
CC       coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC       methionine. {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: Mitochondrion {ECO:0000255|HAMAP-
CC       Rule:MF_03123}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl
CC       synthase family. {ECO:0000255|HAMAP-Rule:MF_03123}.
DR   EMBL; AM920435; CAP85649.1; -; Genomic_DNA.
DR   RefSeq; XP_002562872.1; XM_002562826.1.
DR   SMR; B6HFQ1; -.
DR   STRING; 1108849.XP_002562872.1; -.
DR   EnsemblFungi; CAP85649; CAP85649; PCH_Pc20g03200.
DR   GeneID; 8317549; -.
DR   KEGG; pcs:Pc20g03200; -.
DR   eggNOG; KOG2672; Eukaryota.
DR   eggNOG; COG0320; LUCA.
DR   HOGENOM; HOG000235998; -.
DR   KO; K03644; -.
DR   OMA; PYCDIDF; -.
DR   OrthoDB; 610833at2759; -.
DR   BioCyc; PCHR:PC20G03200-MONOMER; -.
DR   UniPathway; UPA00538; UER00593.
DR   Proteomes; UP000000724; Contig Pc00c20.
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: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; IPR031691; LIAS_N.
DR   InterPro; IPR003698; Lipoyl_synth.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR10949; PTHR10949; 1.
DR   Pfam; PF16881; LIAS_N; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF005963; Lipoyl_synth; 1.
DR   SFLD; SFLDF00271; lipoyl_synthase; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00510; lipA; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HFQ1.
DR   SWISS-2DPAGE; B6HFQ1.
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Mitochondrion; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Transit peptide.
FT   TRANSIT       1     33       Mitochondrion. {ECO:0000255|HAMAP-
FT                                Rule:MF_03123}.
FT   CHAIN        34    416       Lipoyl synthase, mitochondrial.
FT                                /FTId=PRO_5000409605.
FT   METAL       132    132       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_03123}.
FT   METAL       137    137       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_03123}.
FT   METAL       143    143       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_03123}.
FT   METAL       163    163       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_03123}.
FT   METAL       167    167       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_03123}.
FT   METAL       170    170       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_03123}.
SQ   SEQUENCE   416 AA;  45966 MW;  E9F9AE2F5E90A7CA CRC64;
     MAAPTRSLRR LSSFRTTISP SLTVTAPIGC RSYATTDSSS ATNTPGTTRR RATKFQDKLN
     AGPSFSDFVS GGQDEPLDPS EAYALKTALV GPAGRKKEMT RLPEWLKTPI PDSKNYQRLK
     KDLRGLNLHT VCEEARCPNI SDCWGGSDKS SATATIMLMG DTCTRGCRFC SVKTSRAPPP
     LDPHEPENTA EAISRWSLGY VVLTSVDRDD LVDGGARHFA ETVIKIKQKK PSMLVECLTG
     DFRGDTEMAA LVARSGLDVY AHNVETVEEL TPFVRDRRAT FQQSIRVLDS AKKAVPELVT
     KTSLMLGLGE TDEQLWDALR QLRAVNVDVV TFGQYMRPTK RHMAVHEYVT PDRFELWRQR
     ALDMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRAGSGTA ERTVDQTAAT TDEATR
//

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