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B7G3Y9 (LIPA2_PHATC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 32. 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 2, mitochondrial

EC=2.8.1.8
Alternative name(s):
Lipoate synthase 2
Short name=LS 2
Short name=Lip-syn 2
Lipoic acid synthase 2
Gene names
ORF Names:PHATRDRAFT_28652
OrganismPhaeodactylum tricornutum (strain CCAP 1055/1) [Reference proteome]
Taxonomic identifier556484 [NCBI]
Taxonomic lineageEukaryotaStramenopilesBacillariophytaBacillariophyceaeBacillariophycidaeNaviculalesPhaeodactylaceaePhaeodactylum

Protein attributes

Sequence length314 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 By similarity 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)
   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? – 314Lipoyl synthase 2, mitochondrial HAMAP-Rule MF_03123PRO_0000398244

Sites

Metal binding461Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding511Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding571Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding721Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding761Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding791Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B7G3Y9 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 70E379E29A535340

FASTA31434,862
        10         20         30         40         50         60 
MPKGRPSWFK VPAPSQGTQS TYSTASYSRY AQVKDSLQKL DLHTVCEEAQ CPNIGECWNG 

        70         80         90        100        110        120 
GTGTIMLLGD TCTRGCMFCA VNTDSKPPPP DPFEPFKTAE AVVAWGVDYI VLTSVDRDDI 

       130        140        150        160        170        180 
ADGGAQHFAQ TVQLLKQNKP NLLVECLVSD FQGMLDSVET LALSGLDVYA HNVETVERLQ 

       190        200        210        220        230        240 
PFVRDARANY QQSLSTLQHA KVVKPELYTK TSIMLGLGET EEEVTQTMTD LRAIGVDVVT 

       250        260        270        280        290        300 
FGQYLRPTEH HLSVVEYVTP EKFDHYRQVG ENMGFKYVAS GPMVRSSYKA GEFYLEHMIK 

       310 
KERTEAAIDI GENA 

« 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
CM000615 Genomic DNA. Translation: EEC46905.1.
RefSeqXP_002181691.1. XM_002181655.1.
UniGenePtc.241.

3D structure databases

ProteinModelPortalB7G3Y9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING2850.JGI28652.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsPhatr28652; Phatr28652; Phatr28652.
GeneID7202486.
KEGGpti:PHATRDRAFT_28652.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.

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 nameLIPA2_PHATC
AccessionPrimary (citable) accession number: B7G3Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 10, 2009
Last modified: June 11, 2014
This is version 32 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