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Protein

Lipoyl synthase 2, mitochondrial

Gene

LIP1-2

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 1, mitochondrial (LIP1-1), Lipoyl synthase 2, mitochondrial (LIP1-2)
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 bindingi109Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi114Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi120Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi140Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi144Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi147Iron-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 synthase 2, mitochondrial (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthase 2UniRule annotation
Short name:
LS 2UniRule annotation
Short name:
Lip-syn 2UniRule annotation
Lipoic acid synthase 2UniRule annotation
Gene namesi
Name:LIP1-2UniRule annotation
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003988521 – 376Lipoyl synthase 2, mitochondrialAdd BLAST376

Structurei

3D structure databases

ProteinModelPortaliQ3LSN5.
SMRiQ3LSN5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
MF_03128. Lipoyl_synth_plantM. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
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.

Q3LSN5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMYSRFRTVA GNLNCAAKRL SSSSTTTTTT SAPSELQQNL AALRARLAME
60 70 80 90 100
SPSLSDFISL KSDNAYSVEV GTKKKPLPKP KWMKESIPGG EKYVQIKKKL
110 120 130 140 150
RELKLHTVCE EAKCPNLGEC WSGGETGTAT ATIMILGDTC TRGCRFCNVK
160 170 180 190 200
TSRTPPPPDP DEPTNVAEAI ASWGLDYVVI TSVDRDDLPD QGSGHFTETV
210 220 230 240 250
QKLKALKPSM LIEALVPDFR GNAECVEKVS KSGLDVFAHN IETVEELQSA
260 270 280 290 300
VRDHRANFKQ SLDVLMMAKE YAPAGTLTKT SIMLGCGETP DQIVKTMEKV
310 320 330 340 350
RAAGVDVMTF GQHMRPSKRH MPVSEYITPE AFEKYQTLGM EMGFRYVASG
360 370
PMVRSSYKAG EFYIKSMIDS DRAASS
Length:376
Mass (Da):41,294
Last modified:October 25, 2005 - v1
Checksum:i3613E2F6A0492FAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ181623 mRNA. Translation: ABA29155.1.

Similar proteinsi

Entry informationi

Entry nameiLIAS2_PEA
AccessioniPrimary (citable) accession number: Q3LSN5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 25, 2005
Last modified: October 25, 2017
This is version 49 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

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