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D0NP70 (LIPA_PHYIT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 26. 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:PITG_14852
OrganismPhytophthora infestans (strain T30-4) (Potato late blight fungus) [Reference proteome]
Taxonomic identifier403677 [NCBI]
Taxonomic lineageEukaryotaStramenopilesOomycetesPeronosporalesPhytophthora

Protein attributes

Sequence length383 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
Reference 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 – 1919Mitochondrion Potential
Chain20 – 383364Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398245

Sites

Metal binding1161Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1211Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1271Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1471Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1511Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1541Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
D0NP70 [UniParc].

Last modified December 15, 2009. Version 1.
Checksum: 6D29FBE4DC34315F

FASTA38342,420
        10         20         30         40         50         60 
MHASTLTRCM RVAQNARCLS TAAASVQVTH SERGARLAAL RERLAEETRQ GPTFAEQALS 

        70         80         90        100        110        120 
LEDFAFEADA APGTKPSRKP NASNRKPKWL KAQPTQGANY ERLRKSVKSL GLSTVCEEAK 

       130        140        150        160        170        180 
CPNIGECWGG GKDGIATATI MLMGDTCTRG CSFCAVKTSR KPKPLDIEEP NKVAEAIAAW 

       190        200        210        220        230        240 
GLDYIVFTSV DRDDYEDLGA GHFAKTVSTL RAKLPEILIE CLTPDFQGHD NLIDQVATSG 

       250        260        270        280        290        300 
LDVFAHNMET VERLQRRVRD YRANYKQSLH VLERAKVAAP HLVTKTSLML GVGERNEDLF 

       310        320        330        340        350        360 
QTLRDLRNSG VDVVTFGQYL RPSTKHMPVK SYVTPEAFAE WQKVAEQMGF LYVASGPMVR 

       370        380 
SSYKAGEFFM KNLLKNRKTQ VVA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS028150 Genomic DNA. Translation: EEY62412.1.
RefSeqXP_002899048.1. XM_002899002.1.
UniGenePin.6624.

3D structure databases

ProteinModelPortalD0NP70.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsPITG_14852T0; PITG_14852T0; PITG_14852.
GeneID9467967.
KEGGpif:PITG_14852.

Phylogenomic databases

HOGENOMHOG000235998.
KOK03644.
OMAEEYVTPE.

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_PHYIT
AccessionPrimary (citable) accession number: D0NP70
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 15, 2009
Last modified: February 19, 2014
This is version 26 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