(data stored in ACNUC7421 zone)

SWISSPROT: LIPA_SHISS

ID   LIPA_SHISS              Reviewed;         321 AA.
AC   Q3Z4G4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 87.
DE   RecName: Full=Lipoyl synthase {ECO:0000255|HAMAP-Rule:MF_00206};
DE            EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00206};
DE   AltName: Full=Lip-syn {ECO:0000255|HAMAP-Rule:MF_00206};
DE            Short=LS {ECO:0000255|HAMAP-Rule:MF_00206};
DE   AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_00206};
DE   AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00206};
DE   AltName: Full=Sulfur insertion protein LipA {ECO:0000255|HAMAP-Rule:MF_00206};
GN   Name=lipA {ECO:0000255|HAMAP-Rule:MF_00206};
GN   OrderedLocusNames=SSON_0582;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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_00206}.
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_00206};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00206};
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_00206};
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_00206}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00206}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl
CC       synthase family. {ECO:0000255|HAMAP-Rule:MF_00206}.
DR   EMBL; CP000038; AAZ87348.1; -; Genomic_DNA.
DR   SMR; Q3Z4G4; -.
DR   EnsemblBacteria; AAZ87348; AAZ87348; SSON_0582.
DR   KEGG; ssn:SSON_0582; -.
DR   HOGENOM; HOG000235997; -.
DR   KO; K03644; -.
DR   OMA; PYCDIDF; -.
DR   BioCyc; SSON300269:G1GL2-683-MONOMER; -.
DR   UniPathway; UPA00538; UER00593.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00510; lipA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3Z4G4.
DR   SWISS-2DPAGE; Q3Z4G4.
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    321       Lipoyl synthase.
FT                                /FTId=PRO_1000012284.
FT   METAL        68     68       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00206}.
FT   METAL        73     73       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00206}.
FT   METAL        79     79       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00206}.
FT   METAL        94     94       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_00206}.
FT   METAL        98     98       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_00206}.
FT   METAL       101    101       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_00206}.
SQ   SEQUENCE   321 AA;  36072 MW;  BE7BF32A4E3AA358 CRC64;
     MSKPIVMERG VKYRDADKMA LIPVKNVATE REALLRKPEW MKIKLPADST RIQGIKAAMR
     KNGLHSVCEE ASCPNLAECF NHGTATFMIL GAICTRRCPF CDVAHGRPVA PDANEPVKLA
     QTIADMALRY VVITSVDRDD LRDGGAQHFA DCITAIREKS PQIKIETLVP DFRGRMDRAL
     DILTATPPDV FNHNLENVPR IYRQVRPGAD YNWSLKLLER FKEAHPEIPT KSGLMVGLGE
     TNEEIIEVMR DLRRHGVTML TLGQYLQPSR HHLPVQRYVS PDEFDEMKAE ALAMGFTHAA
     CGPFVRSSYH ADLQAKGMEV K
//

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