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Q0A8A4 (LIPA_ALKEH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:Mlg_1586
OrganismAlkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

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 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 – 331331Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325225

Sites

Metal binding721Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding771Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding831Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding981Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1021Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1051Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0A8A4 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: C445EB2010B2D8F2

FASTA33136,573
        10         20         30         40         50         60 
MPTLKGIPVV TSGMKVERDG VRAIKDGVKH NPRAEAAPRG RKPSWLRARV PSGEGYQAVR 

        70         80         90        100        110        120 
DIVRTHRLST VCEESHCPNI GECWNAGTAT IMLMGAVCTR ACRFCAVDTG NPKGRLDHDE 

       130        140        150        160        170        180 
PAHAADSVRL MGLSYVVLTS VDRDDLEDGG AGHYAACVNA IREVNPETAV EVLTPDFNGV 

       190        200        210        220        230        240 
PEHVHRVVDA RPEVFAQNVE TVRRLTHPVR DPRAGYEQTL EVLRLAKARR PDMLTKTSLM 

       250        260        270        280        290        300 
LGLGERDEEI RETLEDLRAV GVDIVTFGQY LQPTRNHLPV ERYVSPAEFA DYRRMGLEMG 

       310        320        330 
FLEVVAGPMV RSSYRADKVL EKNNVGLESA S 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000453 Genomic DNA. Translation: ABI56933.1.
RefSeqYP_742423.1. NC_008340.1.

3D structure databases

ProteinModelPortalQ0A8A4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187272.Mlg_1586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI56933; ABI56933; Mlg_1586.
GeneID4268557.
KEGGaeh:Mlg_1586.
PATRIC20862431. VBIAlkEhr114327_1588.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycAEHR187272:GHAX-1628-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_ALKEH
AccessionPrimary (citable) accession number: Q0A8A4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 60 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