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A9IS79 (LIPA_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:BT_0866
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length320 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 – 320320Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000077949

Sites

Metal binding591Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding641Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding701Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding851Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding891Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding921Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A9IS79 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 856F51B4415321E1

FASTA32036,153
        10         20         30         40         50         60 
MVTVVDRVTN RRLRHPEKAH RPDTSVQKKP DWIRVKAPTS PVYKETHGIV RTHKLVTVCE 

        70         80         90        100        110        120 
EAGCPNIGEC WSQRHASFMI LGEICTRACA FCNVATGIPL AVDDDEPERV ADAVARMELK 

       130        140        150        160        170        180 
HVVITSVDRD DLADGGAEHF AKVIYAIRRK APKTTIEVLT PDFRHKDGAL EVVVAAKPDV 

       190        200        210        220        230        240 
FNHNLETVPS KYLKVRPGAR YFHSIRLLQR VKELDPTIFT KSGIMVGLGE ERNEILQLMD 

       250        260        270        280        290        300 
DLRTADVDFM TIGQYLQPTR KHHPVIRFVP PEEFESFAKI GKVKGFLHMA SNPLTRSSHH 

       310        320 
AGDDFAILQK ARDEKFALQR 

« Hide

References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260525 Genomic DNA. Translation: CAK01271.1.
RefSeqYP_001609266.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9IS79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382640.Btr_0866.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5829176.
KEGGbtr:Btr_0866.
PATRIC20549490. VBIBarTri113218_0903.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000022741.
KOK03644.
OMAHPHIPTK.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycBTRI382640:GJEK-769-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_BART1
AccessionPrimary (citable) accession number: A9IS79
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 47 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