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

B3SBB5 (LIAS_TRIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 35. 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:TRIADDRAFT_38449
OrganismTrichoplax adhaerens (Trichoplax reptans) [Reference proteome]
Taxonomic identifier10228 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlacozoaTrichoplax

Protein attributes

Sequence length350 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? – 350Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398298

Sites

Metal binding831Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding881Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding941Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1131Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1171Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1201Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B3SBB5 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 6DAE3B6F9A2227DE

FASTA35038,945
        10         20         30         40         50         60 
MPSTVASIRD YSNIPKSKRE EIANGPGLED FIVKSPTSLN TLFIYYSNFS LPLPPWLKTT 

        70         80         90        100        110        120 
IPTSNSYNKL NKDLRNLKLH TVCEEARCPN IGECWGGESG TATATIMVLG DTCTRGCRFC 

       130        140        150        160        170        180 
SVKTARKPPP PDPDEPVNTA IALAQWGLDY VVLTSVDRDD LSDGGSNHFA ETVKEIKKRN 

       190        200        210        220        230        240 
LSMLVETLTP DFRGDKAAIA TVVNAGVDVY AHNVETVKNL QWLVRDPRAN YEQSLEVLSY 

       250        260        270        280        290        300 
AKIVNPNLVT KTSIMLGLGE TDESILQTMK DLRSIDVDCI TLGQYMQPTR YHIKVKEYVT 

       310        320        330        340        350 
PAKFQHWEKV GNELGFAYTA SGPLVRSSYK AGEFYLKNLV HKRNKTNGSD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS985264 Genomic DNA. Translation: EDV19926.1.
RefSeqXP_002117516.1. XM_002117480.1.

3D structure databases

ProteinModelPortalB3SBB5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10228.JGI38449.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaTriadT38449; TriadP38449; TriadG38449.
GeneID6758779.
KEGGtad:TRIADDRAFT_38449.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAHPHIPTK.
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_TRIAD
AccessionPrimary (citable) accession number: B3SBB5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 2, 2008
Last modified: June 11, 2014
This is version 35 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