Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B7FRU7 (LIPA1_PHATC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 30. 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
ORF Names:PHATRDRAFT_18029
OrganismPhaeodactylum tricornutum (strain CCAP 1055/1) [Reference proteome]
Taxonomic identifier556484 [NCBI]
Taxonomic lineageEukaryotaStramenopilesBacillariophytaBacillariophyceaeBacillariophycidaeNaviculalesPhaeodactylaceaePhaeodactylum

Protein attributes

Sequence length401 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_03123

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_03123

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_03123

Subcellular location

Mitochondrion Potential HAMAP-Rule MF_03123.

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
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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 – 2525Mitochondrion Potential
Chain26 – 401376Lipoyl synthase 1, mitochondrial HAMAP-Rule MF_03123
PRO_0000398243

Sites

Metal binding1171Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1221Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1281Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1481Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1521Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1551Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B7FRU7 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: C5270EA0E1E231A9

FASTA40144,192
        10         20         30         40         50         60 
MWSSSSSLCR NPSFRRAWLS TVTVTQTAAP TSSRLAALRT QLATEEASID DFSSTNAPTT 

        70         80         90        100        110        120 
TTHYTSSNGS PIVRQKAAPR SAKILPKPRW LKAAPATSDN YRKLRDTVRE LGLATVCEEA 

       130        140        150        160        170        180 
RCPNIGECWG GGEDQTATAT IMIMGDTCTR GCRFCSVKTS RAPPPLDPHE PEKVATAIAQ 

       190        200        210        220        230        240 
WGLDYVVLTS VDRDDLPDQG ADHFRQVVTQ LKLKKPSLLV EALTPDFQGN MDLVHAVATS 

       250        260        270        280        290        300 
GLDVYAHNME TVEALTPKVR DRRATYRQSL EVLRYVKTIQ SDPIGTTNNH NNNNGCLTKT 

       310        320        330        340        350        360 
SLMLGLGETD DQVLTTLRDL RDADVDVVTF GQYLQPTKKH LPVQEYVTPE KFDFWQETAM 

       370        380        390        400 
GMGFAYVASG PLVRSSYKAG ELFLQKYIAQ KKQRNAEVAA A 

« Hide

References

« Hide 'large scale' references
[1]"The Phaeodactylum genome reveals the evolutionary history of diatom genomes."
Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A., Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A., Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T. expand/collapse author list , Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P., Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C., Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D., Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G., La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J., Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A., Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L., Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A., Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R., Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y., Grigoriev I.V.
Nature 456:239-244(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCAP 1055/1.
[2]Diatom Consortium
Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S., Rokhsar D., Bowler C.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: CCAP 1055/1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM000606 Genomic DNA. Translation: EEC50372.1.
RefSeqXP_002177558.1. XM_002177522.1.
UniGenePtc.7635.

3D structure databases

ProteinModelPortalB7FRU7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING2850.JGI18029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsPhatr18029; Phatr18029; Phatr18029.
GeneID7197080.
KEGGpti:PHATRDRAFT_18029.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
ProtClustDBPLN02428.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
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 nameLIPA1_PHATC
AccessionPrimary (citable) accession number: B7FRU7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 10, 2009
Last modified: February 19, 2014
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways