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A4RZ86 (LIAS_OSTLU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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, mitochondrial

EC=2.8.1.8
Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoic acid synthase
Gene names
Name:LIP1
ORF Names:OSTLU_32294
OrganismOstreococcus lucimarinus (strain CCE9901) [Complete proteome]
Taxonomic identifier436017 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaMamiellophyceaeMamiellalesOstreococcus

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 Potential 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
   Technical termComplete proteome
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 – 3030Mitochondrion Potential
Chain31 – 399369Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128
PRO_0000398850

Sites

Metal binding1311Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1361Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1421Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1621Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1691Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A4RZ86 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 2D648EC52BE8F0E5

FASTA39943,907
        10         20         30         40         50         60 
MRAVLELTRR RARNARFARA RAVVGARARA ADAQELRDDS KGGSSVDKAT STAAEARETA 

        70         80         90        100        110        120 
HTLEGFREAL RHGPGFDDFV RGDVAYSVPA PKSLKDKTTR KPAWLKREVP GGERYTEIKS 

       130        140        150        160        170        180 
KLRELKLATV CEEAKCPNLG ECWGGGDGKT ATATIMIMGD TCTRGCRFCA VKTAKAPPPL 

       190        200        210        220        230        240 
DKDEPANVSK AIAAWGLDYV VLTSVDRDDI EDQGAGHFRE TVQRLKASCD VLVEALTPDF 

       250        260        270        280        290        300 
RGEKHLVELV ATSGLDVFAH NVETVPELQR DVRDRRANWD QSIEVLKHAK KSGAKITKTS 

       310        320        330        340        350        360 
IMLGLGETHE QVVNALKLLR EADVDVVTFG QYMRPTKKHL AVVEYVTPEA FKRYQEIAEE 

       370        380        390 
MGFLYVASGA MVRSSYKAGE FFLANVIKQR KAKEAAAAN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000586 Genomic DNA. Translation: ABO96579.1.
RefSeqXP_001418286.1. XM_001418249.1.

3D structure databases

ProteinModelPortalA4RZ86.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436017.A4RZ86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5002530.
KEGGolu:OSTLU_32294.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.
OMADHRLHSV.

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 nameLIAS_OSTLU
AccessionPrimary (citable) accession number: A4RZ86
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 15, 2007
Last modified: May 14, 2014
This is version 50 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