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A5IRA1 (LIPA_STAA9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:SaurJH9_0923
OrganismStaphylococcus aureus (strain JH9) [Complete proteome] [HAMAP]
Taxonomic identifier359786 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length305 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]. 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 – 305305Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000077973

Sites

Metal binding411Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding461Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding521Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding681Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding721Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding751Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A5IRA1 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 0911CD221177702B

FASTA30534,885
        10         20         30         40         50         60 
MATKNEEILR KPDWLKIKLN TNENYTGLKK MMREKNLNTV CEEAKCPNIH ECWGARRTAT 

        70         80         90        100        110        120 
FMILGAVCTR ACRFCAVKTG LPNELDLNEP ERVAESVELM NLKHVVITAV ARDDLRDAGS 

       130        140        150        160        170        180 
NVYAETVRKV RERNPFTTIE ILPSDMGGDY DALETLMASR PDILNHNIET VRRLTPRVRA 

       190        200        210        220        230        240 
RATYDRTLEF LRRSKELQPD IPTKSSIMVG LGETIEEIYE TMDDLRANDV DILTIGQYLQ 

       250        260        270        280        290        300 
PSRKHLKVQK YYTPLEFGKL RKVAMDKGFK HCQAGPLVRS SYHADEQVNE AAKEKQRQGE 


AQLNS 

« Hide

References

[1]"Complete sequence of chromosome of Staphylococcus aureus subsp. aureus JH9."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Tomasz A., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JH9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000703 Genomic DNA. Translation: ABQ48724.1.
RefSeqYP_001246300.1. NC_009487.1.

3D structure databases

ProteinModelPortalA5IRA1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359786.SaurJH9_0923.

Proteomic databases

PRIDEA5IRA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ48724; ABQ48724; SaurJH9_0923.
GeneID5169121.
KEGGsaj:SaurJH9_0923.
PATRIC19539595. VBIStaAur42398_0991.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycSAUR359786:GJEM-948-MONOMER.

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_STAA9
AccessionPrimary (citable) accession number: A5IRA1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 26, 2007
Last modified: February 19, 2014
This is version 54 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