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Q8DLC2 (LIPA2_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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 2

EC=2.8.1.8
Alternative name(s):
Lip-syn 2
Lipoate synthase 2
Lipoic acid synthase 2
Sulfur insertion protein lipA2
Gene names
Name:lipA2
Ordered Locus Names:tll0574
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length290 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
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 – 290290Lipoyl synthase 2 HAMAP-Rule MF_00206
PRO_0000102367

Sites

Metal binding371Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding421Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding481Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding701Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DLC2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 60BE127E2B9A59D9

FASTA29031,735
        10         20         30         40         50         60 
MALSRPLPSW LRKPLGKASE ISTVQRLVRQ YGIHTICEEG RCPNRGECYG QKTATFLLLG 

        70         80         90        100        110        120 
PTCTRACAFC QVEKGHAPAA VDPEEPTKIA AAVATLGLRY VVLTSVARDD LPDQGAGQFV 

       130        140        150        160        170        180 
ATMAAIRQRC PGTEIEVLSP DFRMDRGRLS QRDCIAQIVA AQPACYNHNL ETVRRLQGPV 

       190        200        210        220        230        240 
RRGATYESSL RVLATVKELN PDIPTKSGLM LGLGETEAEI IETLKDLRRV GCDRLTLGQY 

       250        260        270        280        290 
LPPSLSHLPV VKYWTPEEFN TLGNIARELG FSHVRSGPLV RSSYHAAEGG 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC08126.1.
RefSeqNP_681364.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DLC2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tll0574.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC08126; BAC08126; BAC08126.
GeneID1012525.
KEGGtel:tll0574.
PATRIC23926408. VBITheElo119873_0606.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAVQKYWTP.
OrthoDBEOG6038ZS.
ProtClustDBPRK12928.

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 nameLIPA2_THEEB
AccessionPrimary (citable) accession number: Q8DLC2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 71 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