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C4LI04 (LIPA_CORK4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:ckrop_0698
OrganismCorynebacterium kroppenstedtii (strain DSM 44385 / CCUG 35717) [Complete proteome] [HAMAP]
Taxonomic identifier645127 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length347 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 – 347347Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000204145

Sites

Metal binding551Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding601Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding661Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding811Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding851Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding881Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
C4LI04 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 5AAE1555D236514D

FASTA34739,087
        10         20         30         40         50         60 
MAVAPNGRRL LRIEARNAQT PIEAKPRWIR TTATMGPEFR DMKKRVKGAG LHTVCQEAGC 

        70         80         90        100        110        120 
PNIHECWEDR EATFLIGGDT CSRRCDFCDI KSGRPEPLDE DEPRRVAENV REIGLRYSTI 

       130        140        150        160        170        180 
TGVTRDDLPD EGAWLYAEVV RQIHKLNPNT GVENLTPDFS GKPDLLQTVF EARPEVFAHN 

       190        200        210        220        230        240 
LETVPRIFKR IRPAFRYERS LDVIRQARDF GLVTKSNLIL GMGETVDEVK SAMRDLRDAG 

       250        260        270        280        290        300 
CDILTVTQYL RPSNLHHPIE RWVKPEEFVM YRDYGHDIGF AGVMAGPLVR SSYRAGRLYA 

       310        320        330        340 
QAIKARGEEL PANLQHLGEG IDDTASQEAS TLLSKYGASR ETPVGAR 

« Hide

References

[1]"Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385 revealed insights into the physiology of a lipophilic corynebacterium that lacks mycolic acids."
Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P., Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S., Weisshaar B., Goesmann A., Droege M., Puehler A.
J. Biotechnol. 136:22-30(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44385 / CCUG 35717.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001620 Genomic DNA. Translation: ACR17459.1.
RefSeqYP_002906002.1. NC_012704.1.

3D structure databases

ProteinModelPortalC4LI04.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING645127.ckrop_0698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR17459; ACR17459; ckrop_0698.
GeneID7876692.
KEGGckp:ckrop_0698.
PATRIC21516695. VBICorKro120627_0723.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAEWLRRPI.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycCKRO645127:GI7D-690-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_CORK4
AccessionPrimary (citable) accession number: C4LI04
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: May 14, 2014
This is version 39 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