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A6L1U8 (LIPA_BACV8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:BVU_1990
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length284 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 – 284284Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325235

Sites

Metal binding361Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding411Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding471Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding621Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding691Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A6L1U8 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 77A9B74590DFD3A6

FASTA28431,725
        10         20         30         40         50         60 
MNHVKKPDWL KINIGANARY TETKHIVDSH KLHTICSSGR CPNMGECWGK GTATFMIGGE 

        70         80         90        100        110        120 
ICTRSCKFCN TQTGRPLPLD PEEPTHVAES IQLMKLSHAV ITSVDRDDLD DLGAAHWAKT 

       130        140        150        160        170        180 
ISEIKRLNPE TTTEVLIPDF QGKSELIQLV IDAKPDIISH NMETVRRISP LVRSAANYAT 

       190        200        210        220        230        240 
SLKVIKQIAN NGITAKSGIM VGLGERPEEV EEVMDDLLAQ GCKILTIGQY LQPTHRHYPV 

       250        260        270        280 
AEYITPDQFK QYRTIGLKKG FREVESAPLV RSSYHAEKHI KFKG 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000139 Genomic DNA. Translation: ABR39662.1.
RefSeqYP_001299284.1. NC_009614.1.

3D structure databases

ProteinModelPortalA6L1U8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING435590.BVU_1990.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR39662; ABR39662; BVU_1990.
GeneID5302956.
KEGGbvu:BVU_1990.
PATRIC21068890. VBIBacVul85104_2061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAHPHIPTK.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycBVUL435590:GH96-1987-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_BACV8
AccessionPrimary (citable) accession number: A6L1U8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: July 24, 2007
Last modified: May 14, 2014
This is version 55 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