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Q5P4B8 (LIPA_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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:AZOSEA17200
ORF Names:ebA3050
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length315 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 – 315315Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325230

Sites

Metal binding621Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding671Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding731Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding881Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding921Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding951Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P4B8 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 524A8393B53C7E47

FASTA31535,292
        10         20         30         40         50         60 
MDSTARKQRG ADKTARIPIK IVPAERLKKP EWIRIRLGAG HEAERFNEIK ASLREHKLHT 

        70         80         90        100        110        120 
VCEEASCPNI HECFGKGTAT FMIMGDICTR RCPFCDVGHG RPEPLNANEP QELAATIGAM 

       130        140        150        160        170        180 
RLNYVVITSV DRDDLRDGGA QHFVDCIRET RAASPKTRIE VLVPDFRGRL DVALEIFDQA 

       190        200        210        220        230        240 
PPDVMNHNLE TVPRLYKQAR PGADYAYSLR LLKEFKARHP DVPTKSGLMV GLGETDDEIL 

       250        260        270        280        290        300 
DVLRDLRAHD VEMLTIGQYL QPSTGHLPVL RYVHPDTFKM FETEALAMGF KNAACGPMVR 

       310 
SSYWADQQAY GAGVV 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI07845.1.
RefSeqYP_158746.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5P4B8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76114.ebA3050.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI07845; CAI07845; ebA3050.
GeneID3182936.
KEGGeba:ebA3050.
PATRIC20969539. VBIAroAro98752_1726.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycAARO76114:GJTA-1743-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_AROAE
AccessionPrimary (citable) accession number: Q5P4B8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 67 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