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A8Z609 (LIPA_SULMW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:SMGWSS_152
OrganismSulcia muelleri (strain GWSS) [Complete proteome] [HAMAP]
Taxonomic identifier444179 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesCandidatus Sulcia

Protein attributes

Sequence length286 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 – 286286Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325314

Sites

Metal binding381Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding431Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding491Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding641Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding681Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding711Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A8Z609 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: F3A75E08C1789D0B

FASTA28632,985
        10         20         30         40         50         60 
MKKNKNINFK PKWLRVKSPD KYNNIYKISN YNNLNTICKS GSCPNIAECW EQGVATFMIL 

        70         80         90        100        110        120 
GNICTRSCKF CGVKTGKPNK IDFYEPKKIA HNIKIMKIKH AVITSVDRDD LKDMGAIIWG 

       130        140        150        160        170        180 
KTIKAIKNIN EKISLETLIP DFKGRKDLIN IIVNEKPEVI SHNIETVRRL TKKVRTQAKY 

       190        200        210        220        230        240 
DRSINVLKYI KLISNIRTKT GIMLGLGETE EEVIQTLKDS RNANIDIITI GQYLSPSIKH 

       250        260        270        280 
FYVKKFIPPY IFKKYENIAL DMGFLYVESG PLVRSSYNAY KHIFLK 

« Hide

References

[1]"Parallel genomic evolution and metabolic interdependence in an ancient symbiosis."
McCutcheon J.P., Moran N.A.
Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GWSS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000770 Genomic DNA. Translation: ABS30560.1.
RefSeqYP_001597956.1. NC_010118.1.

3D structure databases

ProteinModelPortalA8Z609.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444179.SMGWSS_152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS30560; ABS30560; SMGWSS_152.
GeneID5797165.
KEGGsmg:SMGWSS_152.
PATRIC32019003. VBICanSul12747_0125.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycCSUL444179:GHLI-150-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]
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_SULMW
AccessionPrimary (citable) accession number: A8Z609
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 46 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