(data stored in ACNUC7421 zone)

SWISSPROT: D1CDL2_THET1

ID   D1CDL2_THET1            Unreviewed;       303 AA.
AC   D1CDL2;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   10-APR-2019, entry version 81.
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   OrderedLocusNames=Tter_0096 {ECO:0000313|EMBL:ACZ41018.1}, Tter_2833
GN   {ECO:0000313|EMBL:ACZ43716.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41018.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41018.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 {ECO:0000313|EMBL:ACZ41018.1}, and ATCC BAA-798 /
RC   YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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; CP001825; ACZ41018.1; -; Genomic_DNA.
DR   EMBL; CP001826; ACZ43716.1; -; Genomic_DNA.
DR   RefSeq; WP_012874053.1; NC_013526.1.
DR   STRING; 525904.Tter_2833; -.
DR   EnsemblBacteria; ACZ41018; ACZ41018; Tter_0096.
DR   EnsemblBacteria; ACZ43716; ACZ43716; Tter_2833.
DR   KEGG; ttr:Tter_0096; -.
DR   KEGG; ttr:Tter_2833; -.
DR   eggNOG; ENOG4105C0G; Bacteria.
DR   eggNOG; COG0320; LUCA.
DR   HOGENOM; HOG000235998; -.
DR   KO; K03644; -.
DR   OMA; PYCDIDF; -.
DR   OrthoDB; 1184806at2; -.
DR   BioCyc; TTER525904:G1GGS-2877-MONOMER; -.
DR   BioCyc; TTER525904:G1GGS-96-MONOMER; -.
DR   UniPathway; UPA00538; UER00593.
DR   Proteomes; UP000000323; Chromosome 1.
DR   Proteomes; UP000000323; Chromosome 2.
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; D1CDL2.
DR   SWISS-2DPAGE; D1CDL2.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
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:UP000000323};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   DOMAIN       65    270       Elp3. {ECO:0000259|SMART:SM00729}.
FT   METAL        49     49       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        54     54       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        60     60       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        75     75       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        79     79       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        82     82       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
SQ   SEQUENCE   303 AA;  33986 MW;  2658195E356E3C2B CRC64;
     MKPDVEHMSD GRPAYELPKP SWIKARIPSG PNYQELKGLM RGLGLHTVCE EAHCPNIGDC
     WERRTATFMI LGRVCTRSCG FCAVETGRPP EYDLLEPGRV AMAVSRLGLR HVVVTSVARD
     ELPDGGAEIF ARTIRAIHRR VPGCSVEVLI PDFRGQEDAI RKVVEAGPEI INHNVETVPR
     LHRRVRPQAK YERSLRVLEL AGELGGEVLT KSGLMVGLGE SRQELRDVMR DLRSVGVEIL
     TVGQYLRPSR EHLPVEKYYT PQEFEELKQE ALELGFKHVE SGPLVRSSYH ADQQVSSLLQ
     KAV
//

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