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A0PNH7 (LIPA_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:MUL_1343
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length324 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 – 324324Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000012240

Sites

Metal binding651Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding701Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding761Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding911Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding951Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding981Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PNH7 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 7EB830150D893E88

FASTA32436,021
        10         20         30         40         50         60 
MNVAPEPGAA GAAAPQGRKL LRLEVRNAQT PIERKPPWIR TRARMGPEYT ELKNLVRREG 

        70         80         90        100        110        120 
LHTVCEEAGC PNIFECWEDR EATFLIGGDQ CTRRCDFCQI DTGKPAPLDR DEPRRVAESV 

       130        140        150        160        170        180 
HTMGLRYATV TGVARDDLPD GGAWLYAETV RAIKELNPST GVELLIPDFN GKADQLGEVF 

       190        200        210        220        230        240 
EARPEVLAHN VETVPRVFKR IRPAFTYQRS LDVLTAARQF GLVTKSNLIL GMGETPEEVR 

       250        260        270        280        290        300 
TALVDLHDAG CDIITITQYL RPSPRHHPVE RWVRPEEFVE FAQYAEGLGF AGVLAGPLVR 

       310        320 
SSYRAGRLYE QARSRNTSGA SNSG 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL03896.1.
RefSeqYP_905367.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PNH7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_1343.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL03896; ABL03896; MUL_1343.
GeneID4554083.
KEGGmul:MUL_1343.
PATRIC18169528. VBIMycUlc37413_1620.

Organism-specific databases

GenoListMUL_1343.
CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAHPHIPTK.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

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_MYCUA
AccessionPrimary (citable) accession number: A0PNH7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: May 14, 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