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Q0RFE8 (LIPA_FRAAA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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

EC=2.8.1.8
Alternative name(s):
Lip-syn
Short name=LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA
Gene names
Name:lipA
Ordered Locus Names:FRAAL5157
OrganismFrankia alni (strain ACN14a) [Complete proteome] [HAMAP]
Taxonomic identifier326424 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeFrankiaceaeFrankia

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
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_00206

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_00206

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_00206

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00206.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   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_componentcytoplasm

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

Chain1 – 328328Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000012223

Sites

Metal binding561Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding611Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding671Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding821Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding861Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding891Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0RFE8 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: C72BF5DDF1FA5654

FASTA32836,363
        10         20         30         40         50         60 
MSAVAPEGRP LLRLEARNAQ TPIERKPPWI RTRMRTGPEY SDVKGLVRAA GLHTVCEEAG 

        70         80         90        100        110        120 
CPNIYECWED REATFLIGGD VCTRRCDFCQ IDSGRPTPLD RDEPRRVAES VRTMGLRYAT 

       130        140        150        160        170        180 
VTGVARDDLA DGGSWLYGET VRQIHALSAG TGVEVLIPDF GGRADQLDEV FGAAPEVLAH 

       190        200        210        220        230        240 
NLETVPRIFK RIRPAFRYER SLDVLRQARA AGLVTKSNLI LGLGETAEEI HAAMRDLHAA 

       250        260        270        280        290        300 
GCELLTVTQY LRPTPRHHPV ERWVRPEEFL DWERVGAELG FSGVMSGPLV RSSYRAGRLY 

       310        320 
QQAITARGEG HTAASDLPKS VLETSHTQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT573213 Genomic DNA. Translation: CAJ63797.1.
RefSeqYP_715333.1. NC_008278.1.

3D structure databases

ProteinModelPortalQ0RFE8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326424.FRAAL5157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4237486.
KEGGfal:FRAAL5157.
PATRIC21919546. VBIFraAln347_4727.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycFALN326424:GJ82-5081-MONOMER.
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_FRAAA
AccessionPrimary (citable) accession number: Q0RFE8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: February 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways