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Lipoyl synthase (EC 2.8.1.8) (Lip-syn) (LS) (Lipoate synthase) (Lipoic acid synthase) (Sulfur insertion protein LipA)

 Q1PJD6_PROMR            Unreviewed;       297 AA.
Q1PJD6;
16-MAY-2006, integrated into UniProtKB/TrEMBL.
16-MAY-2006, sequence version 1.
25-OCT-2017, entry version 67.
RecName: Full=Lipoyl synthase {ECO:0000256|HAMAP-Rule:MF_00206};
EC=2.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00206};
AltName: Full=Lip-syn {ECO:0000256|HAMAP-Rule:MF_00206};
Short=LS {ECO:0000256|HAMAP-Rule:MF_00206};
AltName: Full=Lipoate synthase {ECO:0000256|HAMAP-Rule:MF_00206};
AltName: Full=Lipoic acid synthase {ECO:0000256|HAMAP-Rule:MF_00206};
AltName: Full=Sulfur insertion protein LipA {ECO:0000256|HAMAP-Rule:MF_00206};
Name=lipA {ECO:0000256|HAMAP-Rule:MF_00206,
ECO:0000313|EMBL:ABE11440.1};
ORFNames=HOT0M-5C8_0010 {ECO:0000313|EMBL:ABE11440.1};
uncultured Prochlorococcus marinus clone HOT0M-5C8.
Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
Prochlorococcus.
NCBI_TaxID=379389 {ECO:0000313|EMBL:ABE11440.1};
[1] {ECO:0000313|EMBL:ABE11440.1}
NUCLEOTIDE SEQUENCE.
PubMed=16556843; DOI=10.1126/science.1122050;
Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
Delong E.F., Chisholm S.W.;
"Genomic islands and the ecology and evolution of Prochlorococcus.";
Science 311:1768-1770(2006).
[2] {ECO:0000313|EMBL:ABE11440.1}
NUCLEOTIDE SEQUENCE.
US DOE Joint Genome Institute (JGI);
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Richardson P.;
"Sequencing of the draft fosmids and assembly of Prochlorococcus
marinus environmental genome fragment.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the radical-mediated insertion of two sulfur
atoms into the C-6 and C-8 positions of the octanoyl moiety bound
to the lipoyl domains of lipoate-dependent enzymes, thereby
converting the octanoylated domains into lipoylated derivatives.
{ECO:0000256|HAMAP-Rule:MF_00206}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(octanoyl)lysine + 2 sulfur-
(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S]
ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2
L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S]
ferredoxin. {ECO:0000256|HAMAP-Rule:MF_00206}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|HAMAP-Rule:MF_00206};
Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is
coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
methionine. {ECO:0000256|HAMAP-Rule:MF_00206};
-!- PATHWAY: Protein modification; protein lipoylation via endogenous
pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
protein]: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00206,
ECO:0000256|SAAS:SAAS00921108}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206}.
-!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl
synthase family. {ECO:0000256|HAMAP-Rule:MF_00206}.
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EMBL; DQ366737; ABE11440.1; -; Genomic_DNA.
ProteinModelPortal; Q1PJD6; -.
UniPathway; UPA00538; UER00593.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0016992; F:lipoate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_00206; Lipoyl_synth; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR006638; Elp3/MiaB/NifB.
InterPro; IPR003698; Lipoyl_synth.
InterPro; IPR007197; rSAM.
Pfam; PF04055; Radical_SAM; 1.
PIRSF; PIRSF005963; Lipoyl_synth; 1.
SFLD; SFLDG01058; lipoyl_synthase_like; 1.
SFLD; SFLDS00029; Radical_SAM; 1.
SMART; SM00729; Elp3; 1.
TIGRFAMs; TIGR00510; lipA; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00206};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206};
Iron {ECO:0000256|HAMAP-Rule:MF_00206};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00206};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00206};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00206};
Transferase {ECO:0000256|HAMAP-Rule:MF_00206}.
DOMAIN 57 265 Elp3. {ECO:0000259|SMART:SM00729}.
METAL 41 41 Iron-sulfur 1 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_00206}.
METAL 46 46 Iron-sulfur 1 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_00206}.
METAL 52 52 Iron-sulfur 1 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_00206}.
METAL 67 67 Iron-sulfur 2 (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00206}.
METAL 71 71 Iron-sulfur 2 (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00206}.
METAL 74 74 Iron-sulfur 2 (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00206}.
SEQUENCE 297 AA; 33572 MW; DF0CD860B69BF99C CRC64;
MTNISKNAVS KPDWLRVKAP QVERIGNTAN LLSDLKLNTV CQEASCPNIG ECFASGTATF
LIMGPGCTRA CPYCDIDFDR SKRDIDPTEP DRLAEAVYRM KLKHVVITSV NRDDLEDGGA
SQFYKCVAEV RKKSPETTIE LLIPDLCGNW LALEKVLDSK PNVLNHNVET VPALYRKVRP
EGNYQRTLEL LKITREYFPS VYTKSGFMLG LGEKDDEVLN LLMDLRKNDV DIVTIGQYLS
PGPKHLPVQK FISPSKFNYF KLFGENELGF MQVVSSPLTR SSYHAEEIQK LMKKFPR


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