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B2FUS8 (LIPA_STRMK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:Smlt4046
OrganismStenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]
Taxonomic identifier522373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Protein attributes

Sequence length336 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 – 336336Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000099639

Sites

Metal binding811Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding861Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding921Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1071Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1111Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1141Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B2FUS8 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 83B3E094A5041EF8

FASTA33637,044
        10         20         30         40         50         60 
MTETTARSIP LQIVQGDSPS AAPLQAGVKQ LGGDKINRSP VQFADAPVLR KPSWIRVRIP 

        70         80         90        100        110        120 
SGNAVQNLKA KLRENRLVTV CEEASCPNIH ECFGHGTATF MILGEVCTRR CSFCDVAHGR 

       130        140        150        160        170        180 
PKPPDANEPA SLGQTVADMG LKYVVVTSVD RDDLRDGGAQ HFVDCITAIR EKSPGTRIEV 

       190        200        210        220        230        240 
LTPDFRGKGR MERALEILAQ NPPDVFNHNI ETVPDLYRNV RPGADYQWSL NLLKNFKAQH 

       250        260        270        280        290        300 
PDVPTKSGIM LGLGEDFEQI KATLRDLRAH DVDMITIGQY LQPTAHHHPV LKYWTPEDYK 

       310        320        330 
ALEDYGYELG FSHVASGPMV RSSYHADVQA KGAGVS 

« Hide

References

[1]"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. expand/collapse author list , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K279a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM743169 Genomic DNA. Translation: CAQ47438.1.
RefSeqYP_001973724.1. NC_010943.1.

3D structure databases

ProteinModelPortalB2FUS8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING522373.Smlt4046.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ47438; CAQ47438; Smlt4046.
GeneID6393385.
KEGGsml:Smlt4046.
PATRIC23703533. VBISteMal45202_3816.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAHPHIPTK.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycSMAL522373:GJE8-3907-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_STRMK
AccessionPrimary (citable) accession number: B2FUS8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 45 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