(data stored in ACNUC7421 zone)

SWISSPROT: Q146F1_PARXL

ID   Q146F1_PARXL            Unreviewed;       334 AA.
AC   Q146F1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 100.
DE   RecName: Full=Lipoyl synthase {ECO:0000256|HAMAP-Rule:MF_00206};
DE            EC=2.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00206};
DE   AltName: Full=Lip-syn {ECO:0000256|HAMAP-Rule:MF_00206};
DE            Short=LS {ECO:0000256|HAMAP-Rule:MF_00206};
DE   AltName: Full=Lipoate synthase {ECO:0000256|HAMAP-Rule:MF_00206};
DE   AltName: Full=Lipoic acid synthase {ECO:0000256|HAMAP-Rule:MF_00206};
DE   AltName: Full=Sulfur insertion protein LipA {ECO:0000256|HAMAP-Rule:MF_00206};
GN   Name=lipA {ECO:0000256|HAMAP-Rule:MF_00206};
GN   ORFNames=Bxe_A4212 {ECO:0000313|EMBL:ABE28788.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28788.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28788.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28788.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00206};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00206}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206,
CC       ECO:0000256|SAAS:SAAS01101439}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl
CC       synthase family. {ECO:0000256|HAMAP-Rule:MF_00206}.
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DR   EMBL; CP000270; ABE28788.1; -; Genomic_DNA.
DR   RefSeq; WP_011486629.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4212; -.
DR   EnsemblBacteria; ABE28788; ABE28788; Bxe_A4212.
DR   GeneID; 4004726; -.
DR   KEGG; bxb:DR64_1889; -.
DR   KEGG; bxe:Bxe_A4212; -.
DR   PATRIC; fig|266265.5.peg.264; -.
DR   eggNOG; ENOG4105C0G; Bacteria.
DR   eggNOG; COG0320; LUCA.
DR   HOGENOM; HOG000235997; -.
DR   KO; K03644; -.
DR   OMA; PYCDIDF; -.
DR   OrthoDB; 1184806at2; -.
DR   BioCyc; BXEN266265:BXE_RS01245-MONOMER; -.
DR   UniPathway; UPA00538; UER00593.
DR   Proteomes; UP000001817; Chromosome 1.
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   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00510; lipA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q146F1.
DR   SWISS-2DPAGE; Q146F1.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206,
KW   ECO:0000256|SAAS:SAAS01101443};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00206,
KW   ECO:0000313|EMBL:ABE28788.1}.
FT   DOMAIN       97    306       Elp3. {ECO:0000259|SMART:SM00729}.
FT   METAL        81     81       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        86     86       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        92     92       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL       107    107       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL       111    111       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL       114    114       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
SQ   SEQUENCE   334 AA;  36986 MW;  0016BD1AD32668F9 CRC64;
     MTDVTANLAA SPAPDAVPAP AAYDATAKQK AQAKTARIPI KVIPIEKLKK PDWIRVKAAT
     GNSRFYEIKQ ILREHNLHTV CEEASCPNIG ECFGKGTATF MIMGDKCTRR CPFCDVGHGR
     PDPLDADEPG NLARTIAALK LKYVVITSVD RDDLRDGGAA HFVECIRQTR ELSPQTRIEI
     LTPDFRGRLD RALGILNAAP PDVMNHNLET VPRLYKEARP GSDYAHSLKL LKDFKALHPD
     VATKSGLMVG LGETEEEILQ VMRDLREHDV DMLTIGQYLQ PSEHHLPVRS YVHPDTFRMY
     EEEAYKMGFT HAAVGAMVRS SYHADLQAHG AGVV
//

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