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B2WBE8 (LIPA_PYRTR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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:PTRG_06961
OrganismPyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) (Drechslera tritici-repentis) [Complete proteome]
Taxonomic identifier426418 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaePyrenophora

Protein attributes

Sequence length417 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
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 – 3030Mitochondrion Potential
Chain31 – 417387Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398285

Sites

Metal binding1321Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1431Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1701Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B2WBE8 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 56EB27FD34072E72

FASTA41746,079
        10         20         30         40         50         60 
MATSIPRSRC FLTSSTLKVV PRSRTPLRSF ATTSDTPQTS VPEAPGKRSR PPTSFSDTLN 

        70         80         90        100        110        120 
AGPSFGDFVN PNAPLSPTEA YEIKTVQVGP EGRKKTITRL PEWLRTPIPS NANQNYKQIK 

       130        140        150        160        170        180 
KDLRGLNLAT VCEEARCPNI SDCWGGSSKS AATATIMLMG DTCTRGCRFC AVKTSKAPPP 

       190        200        210        220        230        240 
LDPHEPENTA EALRRWGLGY VVITVVDRDD LADSGAHHIA ETIMKIKQKN PTQLVELLGG 

       250        260        270        280        290        300 
DYGGNLEMAK VVARSGVDVF AHNIETTERL TPFVRDRRAK FRQSLDVLRS AKEERPELIT 

       310        320        330        340        350        360 
KTSMMLGLGE TDEDLWHALR ELRANNVDVV TFGQYMRPTK RHMAVHDYVT PDKFELWRQR 

       370        380        390        400        410 
ALDMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRLGSSAG KNDVAELSAA EEVGKAL 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS231621 Genomic DNA. Translation: EDU49880.1.
RefSeqXP_001937293.1. XM_001937258.1.

3D structure databases

ProteinModelPortalB2WBE8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEDU49880; EDU49880; PTRG_06961.
GeneID6345232.

Phylogenomic databases

OrthoDBEOG79KPR7.

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 nameLIPA_PYRTR
AccessionPrimary (citable) accession number: B2WBE8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways