Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5LGU6 (LIPA_BACFN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:BF0898
OrganismBacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]
Taxonomic identifier272559 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length288 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 – 288288Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325234

Sites

Metal binding391Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding441Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding501Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding651Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding691Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding721Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LGU6 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 48A0ED0A235CB9C3

FASTA28832,108
        10         20         30         40         50         60 
MGNDKRVRKP EWLKISIGAN ERYTETKRIV ESHCLHTICS SGRCPNMGEC WGKGTATFMI 

        70         80         90        100        110        120 
AGDICTRSCK FCNTQTGRPL PLDPDEPTHV AESIALMKLS HAVITSVDRD DLPDLGAAHW 

       130        140        150        160        170        180 
AQTIREIKRL NPETTTEVLI PDFQGRKELV DQVIKACPEI ISHNMETVKR ISPQVRSAAN 

       190        200        210        220        230        240 
YHTSLEVIRQ IAESGITAKS GIMVGLGETP AEVEELMDDL ISVGCKILTI GQYLQPTHKH 

       250        260        270        280 
FPVAAYITPE QFAVYKETGL KKGFEQVESA PLVRSSYHAE KHIRFNNK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR626927 Genomic DNA. Translation: CAH06641.1.
RefSeqYP_210592.1. NC_003228.3.

3D structure databases

ProteinModelPortalQ5LGU6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272559.BF0898.

Protocols and materials databases

DNASU3288526.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH06641; CAH06641; BF9343_0860.
GeneID3288526.
KEGGbfs:BF0898.
PATRIC21038266. VBIBacFra29119_0887.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAPNIAECF.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycBFRA272559:GKF0-873-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_BACFN
AccessionPrimary (citable) accession number: Q5LGU6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 21, 2005
Last modified: May 14, 2014
This is version 65 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