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Protein

Lipoyl synthase, mitochondrial

Gene

Smp_010100

Organism
Schistosoma mansoni (Blood fluke)
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

Miscellaneous

This protein may be expected to contain an N-terminal transit peptide but none has been predicted.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. no protein annotated in this organism
  2. Lipoyl synthase, mitochondrial (Smp_010100)
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 bindingi134Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi139Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi145Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi165Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi169Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi172Iron-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

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
ORF Names:Smp_010100
OrganismiSchistosoma mansoni (Blood fluke)
Taxonomic identifieri6183 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma
Proteomesi
  • UP000008854 Componenti: Chromosome 3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003982291 – 410Lipoyl synthase, mitochondrialAdd BLAST410

Interactioni

Protein-protein interaction databases

STRINGi6183.Smp_010100__mRNA.

Structurei

3D structure databases

ProteinModelPortaliC4PZQ3.
SMRiC4PZQ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
HOGENOMiHOG000235998.
InParanoidiC4PZQ3.
OrthoDBiEOG091G0AXJ.
PhylomeDBiC4PZQ3.

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.
SMARTiView protein in SMART
SM00729. Elp3. 1 hit.
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

C4PZQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLLPRGSY VFPVLASVSA ATKRRAEWSY IKINITHSYS SNDKSSEFEE
60 70 80 90 100
DNPTQKLSPE FQKAIAHGPS LSEFIKLSNN NQSTKEDFFS SPSSVNKSGK
110 120 130 140 150
SLRLPEWLKT EIPCGGSVAR LQKQLRSLNL HTVCEEARCP NISECWTAGK
160 170 180 190 200
STAATATIMI MGDTCTRGCR FCSVKTSPNP PPLDPDEPVN TAEAISKWDV
210 220 230 240 250
DYIVITSVDR DDLGDGGARH IAKTIRQIKV RKPSIIVECL VPDFRGCTDS
260 270 280 290 300
IHTVVRASPE VYAHNIETVE SLQRVVRDHR AGYIQSLRSL ETAKERSNRL
310 320 330 340 350
VSSGDADFLV VTKSSIMLGL GEKEKEVMIA LKDLRQAGVD CVTIGQYVQP
360 370 380 390 400
TKRHLKVKEY IHPDKFDYWA KIGNDLGFLY TASGPLVRSS YRAGEYYIKH
410
IIDQRKRKNI
Length:410
Mass (Da):45,769
Last modified:July 7, 2009 - v1
Checksum:i727583BC7ADF758F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HE601626 Genomic DNA. Translation: CCD78443.1.
RefSeqiXP_018651054.1. XM_018799246.1.

Genome annotation databases

EnsemblMetazoaiSmp_010100.1; Smp_010100.1:pep; Smp_010100.
GeneDBiSmp_010100.1:pep.
GeneIDi8353012.

Similar proteinsi

Entry informationi

Entry nameiLIAS_SCHMA
AccessioniPrimary (citable) accession number: C4PZQ3
Secondary accession number(s): G4VET5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 7, 2009
Last modified: September 27, 2017
This is version 55 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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