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A4RW69 (LISC_OSTLU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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, chloroplastic

EC=2.8.1.8
Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoate synthase, plastidial
Short name=LIP1p
Lipoic acid synthase
Gene names
Name:LIP1P
ORF Names:OSTLU_31232
OrganismOstreococcus lucimarinus (strain CCE9901) [Complete proteome]
Taxonomic identifier436017 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaMamiellophyceaeMamiellalesOstreococcus

Protein attributes

Sequence length324 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_03129

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_03129

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_03129

Subcellular location

Plastidchloroplast HAMAP-Rule MF_03129.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   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_componentchloroplast

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 – ?Chloroplast Potential
Chain? – 324Lipoyl synthase, chloroplastic HAMAP-Rule MF_03129PRO_0000398866

Sites

Metal binding581Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding631Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding691Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding861Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding901Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding931Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A4RW69 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: A494F5444E1D46E5

FASTA32435,487
        10         20         30         40         50         60 
MCGPTATTVA NAGTGGETIK GLPPGLKKPP WLRQRAPSGE RFDYLSESLT GLKLNTVCEE 

        70         80         90        100        110        120 
AMCPNVGECW NGDTGTATVM LLGDTCTRGC RFCAVNTSQT PPPPDENEPE NTAHAIAEWG 

       130        140        150        160        170        180 
VGYIVLTSVD RDDIPDGGSE HFARTVRTLK TIKSSVLVEA LTPDFQGDMN AVAHLARSGL 

       190        200        210        220        230        240 
DVFAHNVETV ERLQKRVRDP RANYEQSLAV LRHAKASKEG LVTKTSIMLG LGEEDEEIKQ 

       250        260        270        280        290        300 
CMRACKEAGV DIFTLGQYLQ PTPQHLPVKE FVTPEKFDFW KAYGEEVIGF RYVASGPLVR 

       310        320 
SSYKAGEFFI ESMLRKDALD RGET 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000584 Genomic DNA. Translation: ABO95567.1.
RefSeqXP_001417274.1. XM_001417237.1.

3D structure databases

ProteinModelPortalA4RW69.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436017.A4RW69.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5001263.
KEGGolu:OSTLU_31232.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.
OMACKEGMIT.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
MF_03129. Lipoyl_synth_plantC.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027526. Lipoyl_synth_chlpt.
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 nameLISC_OSTLU
AccessionPrimary (citable) accession number: A4RW69
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 15, 2007
Last modified: May 14, 2014
This is version 51 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