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Protein

Lipoyl synthase

Gene

lipA

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
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)
  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 bindingi53Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi58Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi64Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi79Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi83Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi86Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciLINT189518:G1GL4-1858-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:LA_2292
OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Taxonomic identifieri189518 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesLeptospiralesLeptospiraceaeLeptospira
Proteomesi
  • UP000001408 Componenti: Chromosome I

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001023231 – 301Lipoyl synthaseAdd BLAST301

Interactioni

Protein-protein interaction databases

STRINGi189518.LA_2292

Structurei

3D structure databases

ProteinModelPortaliQ8F3V7
SMRiQ8F3V7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0G Bacteria
COG0320 LUCA
HOGENOMiHOG000235997
InParanoidiQ8F3V7
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
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.

Q8F3V7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPLKKKPRT HSLQNAPEKP DWLKVKLAFP DPKNNPVAIV RNSLEEKKLN
60 70 80 90 100
TVCESASCPN LNHCWSRKTA TYMLGGDICT RRCSYCDVAS GKPFPLDPEE
110 120 130 140 150
PKRIAESSIA LDLRHVVITS VNRDDLEDGG AAHFAKTVKE IRKGLPDCKI
160 170 180 190 200
ELLIPDLKVK QEALEIIFEC NPDIFNHNLE TVKRLFPEVA PQKRYERSLD
210 220 230 240 250
VLKIASARGF LTKSGLILGM GETLEEVKEC MQDLASVGVS LLTLGQYLQP
260 270 280 290 300
TSTHLPVKEY VVPQVFKDLR IYGKSIGFKG VFSGPLVRSS YHADEQISWN

P
Length:301
Mass (Da):33,724
Last modified:March 1, 2003 - v1
Checksum:i7E06D76826F1FDB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010300 Genomic DNA Translation: AAN49491.1
RefSeqiNP_712473.1, NC_004342.2
WP_001068714.1, NC_004342.2

Genome annotation databases

EnsemblBacteriaiAAN49491; AAN49491; LA_2292
GeneIDi1151635
KEGGilil:LA_2292
PATRICifig|189518.3.peg.2278

Similar proteinsi

Entry informationi

Entry nameiLIPA_LEPIN
AccessioniPrimary (citable) accession number: Q8F3V7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2003
Last modified: May 23, 2018
This is version 94 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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