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Q3LSN4 (LIAS1_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoyl synthase 1, mitochondrial

EC=2.8.1.8
Alternative name(s):
Lipoate synthase 1
Short name=LS 1
Short name=Lip-syn 1
Lipoic acid synthase 1
Gene names
Name:LIP1-1
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_03128

Catalytic activity

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_03128

Cofactor

Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_03128

Subcellular location

Mitochondrion By similarity HAMAP-Rule MF_03128.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 376Lipoyl synthase 1, mitochondrial HAMAP-Rule MF_03128PRO_0000398851

Sites

Metal binding1091Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1141Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1201Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1401Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1471Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3LSN4 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 484934B10E861BDB

FASTA37641,290
        10         20         30         40         50         60 
MMYSRFRTVA GNLNCAAKRL SSSSTTTTTT SAPSELQQNL AALRARLAME SPSLSDFISL 

        70         80         90        100        110        120 
KSDNAYSVEV GTKKKPLPKP KWMKESIPGG EKYVQIKKKL RELKLHTVCE EAKCPNLGEC 

       130        140        150        160        170        180 
WSGGETGTAT ATIMILGDTC TRGCRFCNVK TSRTPPPPDP DEPTNVAEAI ASWGLDYVVI 

       190        200        210        220        230        240 
TSVDRDDLPD QGSGHFTETV QKLKALKPST LIEALVPDFR GNAECVEKVS KSGLDVFAHN 

       250        260        270        280        290        300 
IETVEELQSA VRDHRANFKQ SLDVLMMAKE YAPAGTLTKT SIMLGCGETP DQIVKTMEKV 

       310        320        330        340        350        360 
RAAGVDVMTF GQYMRPSKRH MPVSEYITPE AFEKYQTLGM EMGFRYVASG PMVRSSYKAG 

       370 
EFYIKSMIDS DRAASS 

« Hide

References

[1]Doss R.P., Price R.R.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ181624 mRNA. Translation: ABA29156.1.

3D structure databases

ProteinModelPortalQ3LSN4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
MF_03128. Lipoyl_synth_plantM.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIAS1_PEA
AccessionPrimary (citable) accession number: Q3LSN4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 25, 2005
Last modified: February 19, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways