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Q62N16 (LIPA_BURMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:BMA0052
OrganismBurkholderia mallei (strain ATCC 23344) [Complete proteome] [HAMAP]
Taxonomic identifier243160 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length329 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 – 329329Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000012199

Sites

Metal binding761Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding811Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding871Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1021Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1061Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1091Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q62N16 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 209EA922ADB5BC9A

FASTA32936,459
        10         20         30         40         50         60 
MTDLTATPAP AEPAASAYDP TAKQKAQAKT ARIPIKIVPI EKLKKPEWIR VKAATSSSRF 

        70         80         90        100        110        120 
NEIKTILREH NLHTVCEEAS CPNIGECFGK GTATFMIMGD KCTRRCPFCD VGHGRPDPLD 

       130        140        150        160        170        180 
ADEPKNLART IAALKLKYVV ITSVDRDDLR DGGAGHFVEC IREVREQSPA TRIEILTPDF 

       190        200        210        220        230        240 
RGRLDRALAI LNAAPPDVMN HNLETVPRLY KEARPGSDYA HSLKLLKDFK ALHPDVATKS 

       250        260        270        280        290        300 
GLMVGLGETT DEILQVMRDL RAHDVDMLTI GQYLQPSEHH LPVREYVHPD TFKMYEEEAY 

       310        320 
KMGFTHAAVG AMVRSSYHAD LQAHGAGVV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000010 Genomic DNA. Translation: AAU48954.1.
RefSeqYP_101901.1. NC_006348.1.

3D structure databases

ProteinModelPortalQ62N16.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243160.BMA0052.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU48954; AAU48954; BMA0052.
GeneID3090922.
KEGGbma:BMA0052.
PATRIC19115006. VBIBurMal55007_0045.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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_BURMA
AccessionPrimary (citable) accession number: Q62N16
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: February 19, 2014
This is version 63 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