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P0CO59 (LIPA_CRYNB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 18. 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
Ordered Locus Names:CNBI2500
OrganismCryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans) [Complete proteome]
Taxonomic identifier283643 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length395 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 – 2424Mitochondrion Potential
Chain25 – 395371Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000410135

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 binding1371Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
P0CO59 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 6197D8A04772796D

FASTA39542,938
        10         20         30         40         50         60 
MVKLPSASRI RSLATVPSTA TRAFATVNPT PPAAQPTKSK PRFEKLDDGL TFDDFLSGDV 

        70         80         90        100        110        120 
PPENERVVLG NTKQPRLPSF LKHPIPTGAS YSGIKKELRG LGLHTVCEEA KCPNIGECWG 

       130        140        150        160        170        180 
GGKGNATATI MLMGDQCTRG CRFCSVKTSR APPPLDVHEP ENTAEAISRW GLGYIVLTSV 

       190        200        210        220        230        240 
DRDDLVDGGA AHIASTISKI KQKAPNILVE ALTPDFATKG VNVIHTVASS GLDVFAHNVE 

       250        260        270        280        290        300 
TVERCTPFVR DRRAGFSQSL KVLEEAKKGA KAAGREILTK SSIMLGVGEM EEEIHETLRR 

       310        320        330        340        350        360 
LRASDVDVVT FGQYMRPTKR HMKVDRYVEP EEFAKWKNVA EGMGFLYVAS GPLVRSSYKA 

       370        380        390 
GEFFIENVLK KRRAAAAEHA ASQLSTQPPE IAAKV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAEY01000045 Genomic DNA. Translation: EAL18758.1.
RefSeqXP_773405.1. XM_768312.1.

3D structure databases

ProteinModelPortalP0CO59.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4938210.
KEGGcnb:CNBI2500.

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_CRYNB
AccessionPrimary (citable) accession number: P0CO59
Secondary accession number(s): Q55LW2, Q5K8V7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 11, 2014
This is version 18 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