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B6K4J2 (LIPA_SCHJY) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 28. 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:SJAG_03553
OrganismSchizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast) [Complete proteome]
Taxonomic identifier402676 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length377 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 – 7777Mitochondrion Potential
Chain78 – 377300Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398291

Sites

Metal binding1071Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1121Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1181Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1381Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1421Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1451Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B6K4J2 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 7424BAC10F1E8B2E

FASTA37742,163
        10         20         30         40         50         60 
MFRRGGRILN RRIFGAGISA FRVQGRKCAS DLSKALASGP KFSDFLKGDK EEQLKPEEAY 

        70         80         90        100        110        120 
ELEENVVLPN GSVHKRLPSW LKTKVPLGTN FNKIKNDLRG LNLHTVCEEA RCPNMGECWG 

       130        140        150        160        170        180 
GKDKTRATAT IMLMGDTCTR GCRFCSIKTS RKPPPLDPNE PEKTAEAIKR WGLGYVVLTS 

       190        200        210        220        230        240 
VDRDDLADAG ASHIAKTISL IKSKAPQVLV EALTPDFSGN LDLVSHVAKS GLDVFAHNVE 

       250        260        270        280        290        300 
TVEELTPFVR DRRANFRQSL RVLKHAKSVS PHLITKTSIM LGLGETDEEI EATLGELRKN 

       310        320        330        340        350        360 
EVDVVTFGQY MRPTKRHMKV QAYITPDKFE HWRKRAEELG FLYVASGPLV RSSYKAGEFY 

       370 
LTNILRRRTA AKAQADH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
KE651167 Genomic DNA. Translation: EEB08399.1.
RefSeqXP_002174692.1. XM_002174656.1.

3D structure databases

ProteinModelPortalB6K4J2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEEB08399; EEB08399; SJAG_03553.
GeneID7048812.

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_SCHJY
AccessionPrimary (citable) accession number: B6K4J2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 16, 2008
Last modified: March 19, 2014
This is version 28 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