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Q04T63 (LIPA_LEPBJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:LBJ_1322
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]
Taxonomic identifier355277 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

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_0000325271

Sites

Metal binding541Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding591Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding651Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding801Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding841Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding871Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04T63 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 578BA357D48634CA

FASTA30233,783
        10         20         30         40         50         60 
MINPLKKKPR THFLQKAPEK PDWLKVKLTF PDPKNNPVAI VRNSLEKKKL NTVCESASCP 

        70         80         90        100        110        120 
NLNHCWSRKT ATYMLGGDIC TRRCSYCDVA SGKPSALDRD EPKRVAESAI ALGLKHVVIT 

       130        140        150        160        170        180 
AVNRDDLEDG GAAHFAETVE VVREGLPDCK IELLVPDFKV RPESLEIIFQ CKPDIFNHNV 

       190        200        210        220        230        240 
ETIKRLFPEV APQKKYERSL DVLKIASEKG FLTKSGLILG MGETVEEVKE CMRDLIGVGV 

       250        260        270        280        290        300 
SLLTLGQYLQ PTPTHLPVKS YVLPEVFQEL RIYGKSIGFK GVFSGPLVRS SYHADEQVSW 


NP 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JB197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000350 Genomic DNA. Translation: ABJ75907.1.
RefSeqYP_800665.1. NC_008510.1.

3D structure databases

ProteinModelPortalQ04T63.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355277.LBJ_1322.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ75907; ABJ75907; LBJ_1322.
GeneID4410289.
KEGGlbj:LBJ_1322.
PATRIC22357968. VBILepBor13265_1697.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAPNIAECF.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycLBOR355277:GHYM-1307-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_LEPBJ
AccessionPrimary (citable) accession number: Q04T63
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 14, 2006
Last modified: May 14, 2014
This is version 53 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