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Q6ARK0 (LIPA_DESPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:DP0296
OrganismDesulfotalea psychrophila (strain LSv54 / DSM 12343) [Complete proteome] [HAMAP]
Taxonomic identifier177439 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobulbaceaeDesulfotalea

Protein attributes

Sequence length299 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 – 299299Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325244

Sites

Metal binding451Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding501Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding561Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding711Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding751Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding781Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6ARK0 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 3AE763D3EEF06CDB

FASTA29933,578
        10         20         30         40         50         60 
MACSHQKNEQ MRVGKPKWLR RSLPTGPEYE KIRTLLKGSG LTTVCQEAQC PNQFECYSKG 

        70         80         90        100        110        120 
TATFMIMGDH CTRNCRFCAV AHGPKALPDE DEAERVADAV SLLGLRYAVI TSVTRDDLAD 

       130        140        150        160        170        180 
GGASCFVRVI EAIRKKNPKT LIEVLIPDLA GNWGALQTIL DARPDVLNHN IETVPRLYSV 

       190        200        210        220        230        240 
ARPGAEYRRS LELLREVRRR APQMVTKTGM MLGLGEETEE LYATWQDLRE SDCDILTMGQ 

       250        260        270        280        290 
YLQPTVDHLL VQRFVEPTEF DRLGDVALAK DFLAVASGPF VRSSYEAEKL FRKAELARK 

« Hide

References

[1]"The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments."
Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.
Environ. Microbiol. 6:887-902(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LSv54 / DSM 12343.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR522870 Genomic DNA. Translation: CAG35025.1.
RefSeqYP_064032.1. NC_006138.1.

3D structure databases

ProteinModelPortalQ6ARK0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177439.DP0296.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG35025; CAG35025; DP0296.
GeneID2945112.
KEGGdps:DP0296.
PATRIC21710139. VBIDesPsy67261_0324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycDPSY177439:GJW5-299-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_DESPS
AccessionPrimary (citable) accession number: Q6ARK0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: September 13, 2004
Last modified: February 19, 2014
This is version 65 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