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A4WK38 (LIPA_PYRAR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:
Probable 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:Pars_1184
OrganismPyrobaculum arsenaticum (strain DSM 13514 / JCM 11321) [Complete proteome] [HAMAP]
Taxonomic identifier340102 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length296 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 – 296296Probable lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325323

Sites

Metal binding341Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding391Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding451Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding601Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding641Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A4WK38 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 917D6702E0B7AC22

FASTA29632,853
        10         20         30         40         50         60 
MSALPAWLRV EARSYSEMAK VRSVLSRLGV YTVCEGARCP NVFRCWGEGT ATFMILGEVC 

        70         80         90        100        110        120 
TRACRFCSVR TGNPRGYVDL DEPRRVAEAV RRLGLRYVVV TSVDRDDLPD GGAFQYASAI 

       130        140        150        160        170        180 
REIRRLAPGA LVEVLTPDFR GSREAVETVA EAGPDVFAHN VETVRRLTPL VRDRRASYET 

       190        200        210        220        230        240 
SLRVLKTAKE VGCRLTKSGI MLGLGESFDE VVEVLDDLRK AEVDIVTIGQ YVRPTKSARH 

       250        260        270        280        290 
LPVARWVPLE EFQKLGEVAL SMGFKAVASA PLVRSSYRAE DLYEMALGLR PRAVLV 

« Hide

References

[1]"Complete sequence of Pyrobaculum arsenaticum DSM 13514."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13514 / JCM 11321.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000660 Genomic DNA. Translation: ABP50755.1.
RefSeqYP_001153407.1. NC_009376.1.

3D structure databases

ProteinModelPortalA4WK38.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340102.Pars_1184.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP50755; ABP50755; Pars_1184.
GeneID5055526.
KEGGpas:Pars_1184.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEEYVTPE.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycPARS340102:GHGQ-1198-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_PYRAR
AccessionPrimary (citable) accession number: A4WK38
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 51 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