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Q72RU2 (LIPA_LEPIC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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:LIC_11646
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]
Taxonomic identifier267671 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length301 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 By similarity 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 – 301301Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000102322

Sites

Metal binding531Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding581Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding641Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding791Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding831Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding861Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q72RU2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D2C8CAB824202EB6

FASTA30133,666
        10         20         30         40         50         60 
MNPLKKKPRT HSLQNAPEKP DWLKVKLAFP DPKNNPVAIV RNSLEEKKLN TVCESASCPN 

        70         80         90        100        110        120 
LNHCWSRKTA TYMLGGDICT RRCSYCDVAS GKPFPLDPEE PKRIAESSIA LGLRHVVITS 

       130        140        150        160        170        180 
VNRDDLEDGG AAHFAKTVKE IRKGLPDCKI ELLIPDLKVK QEALEIIFEC NPDIFNHNLE 

       190        200        210        220        230        240 
TVKRLFPEVA PQKRYERSLD VLKIASARGF LTKSGLILGM GETLEEVKEC MQDLASVGVS 

       250        260        270        280        290        300 
LLTLGQYLQP TSTHLPVKEY VVPQVFKDLR IYGKSIGFKG VFSGPLVRSS YHADEQISWN 


P 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016823 Genomic DNA. Translation: AAS70241.1.
RefSeqYP_001604.1. NC_005823.1.

3D structure databases

ProteinModelPortalQ72RU2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267671.LIC11646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS70241; AAS70241; LIC_11646.
GeneID2771666.
KEGGlic:LIC11646.
PATRIC22375649. VBILepInt6257_1989.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK03644.
OMAAHHLPVR.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycLINT267671:GHQI-1643-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_LEPIC
AccessionPrimary (citable) accession number: Q72RU2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 73 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