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B3CQP5 (LIPA_ORITI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:OTT_0086
OrganismOrientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi) [Complete proteome] [HAMAP]
Taxonomic identifier334380 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeOrientia

Protein attributes

Sequence length302 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 – 302302Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000099617

Sites

Metal binding441Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding491Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding551Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding701Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding741Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding771Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B3CQP5 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 9C3EA57A02D1BB7F

FASTA30234,099
        10         20         30         40         50         60 
MCSDKNITAT ALVRPSWLRV KAPFSDEYQS TNELIKSLKL NTVCKEAACP NIGECWSKKH 

        70         80         90        100        110        120 
ATVMILGSIC TRACAFCNVS TGKPEQVDEY EPYRLSEAVM KLGLKHVVIT SVDRDDISDG 

       130        140        150        160        170        180 
GASHFAKCIT YIRERSPSTS IEVLTPDFLR KHDAWKIVAK ARPDVYNHNI ETVPSLYLKV 

       190        200        210        220        230        240 
RPGARYYNSL NLLHQVKIFD SSIFTKSGIM VGLGETKHEV LQVMDDLRAA EVDFLTIGQY 

       250        260        270        280        290        300 
LRPSARHIDV DRYVAPDEFD YYARVAKSKG FLMVSASPLT RSSYHAGEHF EKLKQMRLQN 


II 

« Hide

References

[1]"The whole-genome sequencing of the obligate intracellular bacterium Orientia tsutsugamushi revealed massive gene amplification during reductive genome evolution."
Nakayama K., Yamashita A., Kurokawa K., Morimoto T., Ogawa M., Fukuhara M., Urakami H., Ohnishi M., Uchiyama I., Ogura Y., Ooka T., Oshima K., Tamura A., Hattori M., Hayashi T.
DNA Res. 15:185-199(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ikeda.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008981 Genomic DNA. Translation: BAG39544.1.
RefSeqYP_001936778.1. NC_010793.1.

3D structure databases

ProteinModelPortalB3CQP5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING334380.OTT_0086.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG39544; BAG39544; OTT_0086.
GeneID6338111.
KEGGott:OTT_0086.
PATRIC22826134. VBIOriTsu129072_0104.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycOTSU334380:GC7O-88-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_ORITI
AccessionPrimary (citable) accession number: B3CQP5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: February 19, 2014
This is version 41 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