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A9NNH7 (LIAS_PICSI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 27. 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
Name:LIP1
OrganismPicea sitchensis (Sitka spruce) (Pinus sitchensis)
Taxonomic identifier3332 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaePinalesPinaceaePicea

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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_03128

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_03128

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_03128

Subcellular location

Mitochondrion By similarity HAMAP-Rule MF_03128.

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
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 – ?Mitochondrion Potential
Chain? – 386Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128PRO_0000398853

Sites

Metal binding1151Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1201Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1261Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1461Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1501Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1531Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A9NNH7 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 0FAA92A285A950F8

FASTA38642,579
        10         20         30         40         50         60 
MSINPAFLRR ITWGSKSLHH QFTRCQVRAL SSSVEQTPES TTPALSALRE RLANGGPTLS 

        70         80         90        100        110        120 
DFLTRNLGEE PYSVDVGTKK NPLPKPKWMK AAVPGGDKYT AIKAKLREMN LHTVCEEAKC 

       130        140        150        160        170        180 
PNLGECWSGG ETGTATATIM ILGDTCTRGC RFCAVKTSRT PPPPDPNEPT NVAEAIVSWG 

       190        200        210        220        230        240 
LDYVVLTSVD RDDLPDQGSG HFAKTVQKLK QLKPKMLVEA LVPDFQGNSE CVQKVATSGL 

       250        260        270        280        290        300 
DVFAHNIETV EELQRVVRDH RANFNQSLEV LKMAKTYSPL GVLTKTSVML GCGETPAQVI 

       310        320        330        340        350        360 
ETMEKVREAG VDVITFGQYM RPTKRHMAVS EYVTPEAFEK YQKLGMEMGF RYVASGPMVR 

       370        380 
SSYKAGEFYI KSMIEDDRKK ASSSSI 

« Hide

References

[1]"A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464 high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea sitchensis)."
Ralph S.G., Chun H.J., Kolosova N., Cooper D., Oddy C., Ritland C.E., Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J., Marra M.A., Douglas C.J., Ritland K., Bohlmann J.
BMC Genomics 9:484-484(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF082836 mRNA. Translation: ABK22188.1.

3D structure databases

ProteinModelPortalA9NNH7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
MF_03128. Lipoyl_synth_plantM.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
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 nameLIAS_PICSI
AccessionPrimary (citable) accession number: A9NNH7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 5, 2008
Last modified: March 19, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways