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A7TDI2 (LIAS_NEMVE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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
ORF Names:v1g225637
OrganismNematostella vectensis (Starlet sea anemone) [Reference proteome]
Taxonomic identifier45351 [NCBI]
Taxonomic lineageEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaEdwardsiidaeNematostella

Protein attributes

Sequence length291 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)
   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 – ?Mitochondrion Potential
Chain? – 291Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398226

Sites

Metal binding451Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding501Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding561Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding711Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding751Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding781Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A7TDI2 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 974657A99F1109DE

FASTA29133,132
        10         20         30         40         50         60 
MNTVTENVFP PREPKPKWLR VKLPTGKNYT ELRGLVDKYK LNTICASGSC PNMGECWGEG 

        70         80         90        100        110        120 
TATFMILGNI CTRSCGFCGV KTGRPETVDW DEPEKVARSI KLMKIKHAVI TSVDRDDLKD 

       130        140        150        160        170        180 
MGSIIWAETV KAIRRMNPNT TLETLIPDFQ GNTRNLDRII EVAPEVVSHN METVKRLTRE 

       190        200        210        220        230        240 
VRIQAKYEKS LEVLRYLKAQ GIKRTKSGIM LGLGEKEEEV IQVLHDLRDA NVDIVTIGQY 

       250        260        270        280        290 
LQPSKKHLPV KEYISPEQFE KYEKIGKELG FRHVESGALV RSSYHAEKHI H 

« Hide

References

[1]"Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization."
Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.
Science 317:86-94(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH2 X CH6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS477892 Genomic DNA. Translation: EDO25859.1.
RefSeqXP_001617959.1. XM_001617909.1.

3D structure databases

ProteinModelPortalA7TDI2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING45351.JGI225637.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaNEMVEDRAFT_v1g225637-RA; NEMVEDRAFT_v1g225637-PA; NEMVEDRAFT_v1g225637.
GeneID5496152.
KEGGnve:NEMVE_v1g225637.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAGESHEEI.
OrthoDBEOG7P2XS7.

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 nameLIAS_NEMVE
AccessionPrimary (citable) accession number: A7TDI2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 2, 2007
Last modified: February 19, 2014
This is version 41 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