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C4YA37 (LIPA_CLAL4) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 31. 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:CLUG_04975
OrganismClavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae) [Complete proteome]
Taxonomic identifier306902 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesMetschnikowiaceaeClavispora

Protein attributes

Sequence length391 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)
   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 – 4444Mitochondrion Potential
Chain45 – 391347Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398262

Sites

Metal binding1201Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1251Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1311Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1501Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1541Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1571Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
C4YA37 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: EE362CDEE68AFA88

FASTA39143,682
        10         20         30         40         50         60 
MVHPHLSRTK RTFFSHSSQM ISRHIRKTNS LAFVRALSAS ETAVTPRRKR TVFTDELNKG 

        70         80         90        100        110        120 
PSFEDFVSGK AADVFVDPLE AARKDPEAKL PKWLKVPIPK GRSFHSVKKD VRELKLATVC 

       130        140        150        160        170        180 
EEAKCPNISE CWGGKKSEAT ATIMLLGDTC TRGCRFCSVK TSRTPAKPDP MEPENTAEAI 

       190        200        210        220        230        240 
SRWGLGYVVL TTVDRDDLAD GGAAHLAETV RLIKQKAPQI LVEVLGGDFR GDLTSCDTLA 

       250        260        270        280        290        300 
VSGLDVYAHN LETVEALTPH VRDRRATYRQ SLSILERAKQ AKPSLITKTS LMLGFGETDE 

       310        320        330        340        350        360 
QIMQTLRDLR GIGCDVVTFG QYMRPTKRHM KVVEYVRPEK FDYWKEVALE MGFLYVASGP 

       370        380        390 
LVRSSYKAGE AFIENVLRKR KHNVGDSPRL A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH408081 Genomic DNA. Translation: EEQ40847.1.
RefSeqXP_002614960.1. XM_002614914.1.

3D structure databases

ProteinModelPortalC4YA37.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8495745.
KEGGclu:CLUG_04975.

Phylogenomic databases

KOK03644.
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_CLAL4
AccessionPrimary (citable) accession number: C4YA37
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 2009
Last modified: June 11, 2014
This is version 31 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