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Protein

Lipoyl synthase

Gene

lipA

Organism
Legionella pneumophila (strain Corby)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Protein N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathwayi: protein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Octanoyltransferase (lipB)
  2. Lipoyl synthase (lipA)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi72Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi77Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi83Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi98Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi102Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi105Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionTransferase
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-synUniRule annotation
Short name:
LSUniRule annotation
Lipoate synthaseUniRule annotation
Lipoic acid synthaseUniRule annotation
Sulfur insertion protein LipAUniRule annotation
Gene namesi
Name:lipAUniRule annotation
Ordered Locus Names:LPC_2548
OrganismiLegionella pneumophila (strain Corby)
Taxonomic identifieri400673 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Subcellular locationi

A5IGG3:
  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003252671 – 329Lipoyl synthaseAdd BLAST329

Structurei

3D structure databases

ProteinModelPortaliA5IGG3.
SMRiA5IGG3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000235998.
KOiK03644.
OMAiPYCDIDF.
OrthoDBiPOG091H069D.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
PfamiView protein in Pfam
PF04055. Radical_SAM. 1 hit.
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SFLDiSFLDG01058. lipoyl_synthase_like. 1 hit.
SFLDS00029. Radical_SAM. 1 hit.
SMARTiView protein in SMART
SM00729. Elp3. 1 hit.
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

A5IGG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKLIDIPIV VESGQKYKTS QGVTAIKDGI KSSGQDHERL PKPKWLRIVN
60 70 80 90 100
HTTPAYSQVK EQVQKHRLAT VCEEAKCPNI SECWSHGTAT IMLMGAVCTR
110 120 130 140 150
ACRFCSVDTG NPHGWLDAEE PENTAETVAL MNLDYVVLTS VNRDDLPDGG
160 170 180 190 200
ANHYAKTIRA IKKRSPRTKV EALTPDFQGS ERDVAVLLDS GVDVFAQNVE
210 220 230 240 250
TVERLTHPVR DNRAGYQQTL NVLAFAKKYR PDVLTKTSLM LGLGETDEEI
260 270 280 290 300
IRTMDDLRTH HVDILTLGQY LQPTKNHLPI ARYVTPETFS ELRQIGLKKG
310 320
FFEVASGPLV RSSYRADRVF KRDNLGLDV
Length:329
Mass (Da):36,770
Last modified:June 26, 2007 - v1
Checksum:i36096CB25A28E00B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000675 Genomic DNA. Translation: ABQ56463.1.
RefSeqiWP_011945885.1. NC_009494.2.

Genome annotation databases

EnsemblBacteriaiABQ56463; ABQ56463; LPC_2548.
KEGGilpc:LPC_2548.

Similar proteinsi

Entry informationi

Entry nameiLIPA_LEGPC
AccessioniPrimary (citable) accession number: A5IGG3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 26, 2007
Last modified: October 25, 2017
This is version 68 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families