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A6LE09 (LIPA_PARD8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:BDI_2192
OrganismParabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC 11152) [Complete proteome] [HAMAP]
Taxonomic identifier435591 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaeParabacteroides

Protein attributes

Sequence length281 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 – 281281Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000012250

Sites

Metal binding371Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding421Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding481Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding701Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A6LE09 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: B15D90B412461572

FASTA28131,394
        10         20         30         40         50         60 
MAQHLRKPDW LKIRLGGNEQ FTKTKSIVES HCLHTICTSG KCPNMGECWS RGTATFMIGG 

        70         80         90        100        110        120 
EICTRSCRFC NTLTGKPLPL DPKEPANVAE SIRLMNLKHA VITSVDRDDL PDLGASHWVN 

       130        140        150        160        170        180 
TIRTIKEVNP QTTVEVLIPD FQGRLDLVDQ VVDAAPEIIS HNMETVRRIS PQVRSAAKYD 

       190        200        210        220        230        240 
VSLSVLRRIA ERGVVAKTGI MVGLGETEDE VLELMDDVLQ AGVSVLTIGQ YLQPSRKNIP 

       250        260        270        280 
VSEYVTPERF EYYRQQAVNK GFKKVESAPL VRSSYHAEKH I 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000140 Genomic DNA. Translation: ABR43923.1.
RefSeqYP_001303545.1. NC_009615.1.

3D structure databases

ProteinModelPortalA6LE09.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING435591.BDI_2192.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR43923; ABR43923; BDI_2192.
GeneID5307341.
KEGGpdi:BDI_2192.
PATRIC22847588. VBIParDis29947_2175.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycPDIS435591:GCNH-2186-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_PARD8
AccessionPrimary (citable) accession number: A6LE09
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: February 19, 2014
This is version 50 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