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Q8Y2L3 (LIPA_RALSO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. 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:RSc0322
ORF Names:RS03289
OrganismRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum) [Complete proteome] [HAMAP]
Taxonomic identifier267608 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length333 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 – 333333Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000102345

Sites

Metal binding801Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding851Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding911Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1061Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1101Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1131Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Y2L3 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: A9610E471A778B46

FASTA33337,084
        10         20         30         40         50         60 
MTDSASGASA VANIATPSNE PYDATRKQKS LDKTARIPIK IVPAEKLKKP EWIRVKAATG 

        70         80         90        100        110        120 
NSRFYEIKDI LRANNLVTVC EEASCPNIGE CFGKGTATFM IMGDKCTRRC PFCDVGHGRP 

       130        140        150        160        170        180 
DPLDANEPEN LAKTIAQLRL NYVVITSVDR DDLRDGGAQH YVDCISRTRE LSPATRIEVL 

       190        200        210        220        230        240 
VPDFRGRLEK ALDILQACPP DVMNHNMETV PRLYKQARPG ADYAHSLKLL KDFKARNPNL 

       250        260        270        280        290        300 
PTKSGLMVGL GETDEEILEV MRDMREHDID MLTIGQYLAP SGHHLPVLRY VHPDTFKMFE 

       310        320        330 
EKAYEMGFTH AAVGAMVRSS YHADQQAHEA GFA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL646052 Genomic DNA. Translation: CAD13850.1.
RefSeqNP_518443.1. NC_003295.1.

3D structure databases

ProteinModelPortalQ8Y2L3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267608.RSc0322.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD13850; CAD13850; RSc0322.
GeneID1219125.
KEGGrso:RSc0322.
PATRIC20259187. VBIRalSol70888_0328.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRSOL267608:GCVU-323-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_RALSO
AccessionPrimary (citable) accession number: Q8Y2L3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 82 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