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Q9RWA4 (LIPA_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 105. 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:DR_0765
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length331 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 By similarity 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
Reference 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 – 331331Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000102312

Sites

Metal binding601Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding651Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding711Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding861Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding901Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding931Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RWA4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: AC509CC5A3093397

FASTA33137,037
        10         20         30         40         50         60 
MTQQDPSTKE PKFIKNGIYR KDSVPVREKK PEWLKVTIPT GQVFTEVRKI VKEHRLHTVC 

        70         80         90        100        110        120 
EEAMCPNIGE CWSRGTATFM LMGHICTRAC RFCAVDTGNP MGKLDLDEPR SVADSVRLMD 

       130        140        150        160        170        180 
LKYVVLTSVD RDDLPDGGAY HFAKTVKAIK EVNPQTRVEA LTPDFGGNTA CVDLVLDSGV 

       190        200        210        220        230        240 
DTYAQNLETV RRLTHPVRDI RASYDRTLSV LAHAKQARPD VITKTSLMLG LGETREEIRE 

       250        260        270        280        290        300 
AMADCRAAGV DVLTFGQYLR PTMHHLPVER YISPAEFDEI REEGMQLGFL EVVSGPLVRS 

       310        320        330 
SYKAEQIVMD RPGNLPEHLS HLDGGSELTL I 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF10341.1.
PIRA75480.
RefSeqNP_294489.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RWA4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_0765.

Proteomic databases

PRIDEQ9RWA4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF10341; AAF10341; DR_0765.
GeneID1799433.
KEGGdra:DR_0765.
PATRIC21629078. VBIDeiRad64572_0945.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAHPHIPTK.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycDRAD243230:GH46-787-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_DEIRA
AccessionPrimary (citable) accession number: Q9RWA4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 105 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