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Q30XT6 (LIPA_DESAG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 64. 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:Dde_2714
OrganismDesulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans (strain G20)) [Complete proteome] [HAMAP]
Taxonomic identifier207559 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length291 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 – 291291Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325246

Sites

Metal binding431Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding481Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding541Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding691Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding731Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding761Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30XT6 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 23E55EBB04710EE2

FASTA29132,016
        10         20         30         40         50         60 
MSAQENSAPF LRIPPWLRTR IPCNRTYTAT RELIGDLNLH TVCQSAKCPN MFECFSSRTA 

        70         80         90        100        110        120 
TFLILGGTCT RNCAFCNIEP GDVLPPDAGE PQRVALAAAR LELKHVVITS VTRDDLPDGG 

       130        140        150        160        170        180 
AAHFAATIQA VRSRLPRCTV EVLIPDFQGD AAALQTVLQA RPDVLNHNVE TPPAHYSRIR 

       190        200        210        220        230        240 
PQADYSQSLE LLRRARAAGF TVKSGLMTGL GETDAEVLGV IDDLCATGCN IVTVGQYMRP 

       250        260        270        280        290 
SRRHPAVQRY VHPDMFEEYA AYGRARGIPH MFCAPLVRSS YNASMFVQEK N 

« Hide

References

[1]"Complete genome sequence and updated annotation of Desulfovibrio alaskensis G20."
Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., Nolan M. expand/collapse author list , Lapidus A.L., Palumbo A.V., Wall J.D.
J. Bacteriol. 193:4268-4269(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000112 Genomic DNA. Translation: ABB39510.1.
RefSeqYP_389205.1. NC_007519.1.

3D structure databases

ProteinModelPortalQ30XT6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING207559.Dde_2714.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB39510; ABB39510; Dde_2714.
GeneID3757737.
KEGGdde:Dde_2714.
PATRIC21744371. VBIDesDes50040_2681.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAHIATIGQ.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycDALA207559:GH1L-2429-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_DESAG
AccessionPrimary (citable) accession number: Q30XT6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 64 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