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Protein

Lipoyl synthase

Gene

lipA

Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Status
Reviewed-Annotation score: -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 + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = protein N6-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [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), Octanoyltransferase (lipB)
  2. Lipoyl synthase (lipA), 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

BioCyciFTUL177416:G1G1C-742-MONOMER
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:FTT_0653
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000001174 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003252541 – 327Lipoyl synthaseAdd BLAST327

Interactioni

Protein-protein interaction databases

IntActiQ5NH21, 3 interactors
STRINGi177416.FTT_0653

Structurei

3D structure databases

ProteinModelPortaliQ5NH21
SMRiQ5NH21
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0G Bacteria
COG0320 LUCA
HOGENOMiHOG000235998
KOiK03644
OMAiPYCDIDF

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
IPR031691 LIAS_N
IPR003698 Lipoyl_synth
IPR007197 rSAM
PfamiView protein in Pfam
PF16881 LIAS_N, 1 hit
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.

Q5NH21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEISGIKVK VESGSKYTTD HGFHAVKDGI RNKKENAVHV RKPDWLKVQK
60 70 80 90 100
QDSKEYLKVK SITKKHKLST VCEEARCPNI NECWSHGTAT IMLMGSVCTR
110 120 130 140 150
ACKFCSVDTG NPKGWLDKDE PMNAAESVKL MGLEYVVLTS VDRDDLEDGG
160 170 180 190 200
AGHYAATITA IKNLDENIKV EALTPDFAGI NENIDKIINT KVDVIAQNIE
210 220 230 240 250
TVERLTHPVR DPRAGYWQTL NFLKYVKQKS PNVLTKTSIM VGLGETDEEI
260 270 280 290 300
YKTMDDARSV GVDIITLGQY MQPTKHHLSV ERFVTPQQFE EYRKVGLEKG
310 320
FLEVASGPMV RSSYRADRVF KRNNLDL
Length:327
Mass (Da):36,840
Last modified:February 1, 2005 - v1
Checksum:i5B8D410380E8E6ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA Translation: CAG45286.1
RefSeqiWP_003018819.1, NZ_CP010290.1
YP_169671.1, NC_006570.2

Genome annotation databases

EnsemblBacteriaiCAG45286; CAG45286; FTT_0653
GeneIDi3190780
KEGGiftu:FTT_0653

Similar proteinsi

Entry informationi

Entry nameiLIPA_FRATT
AccessioniPrimary (citable) accession number: Q5NH21
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: February 1, 2005
Last modified: May 23, 2018
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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