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B0R7C4 (LIPA_HALS3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:
Probable 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:OE_4111F
OrganismHalobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) [Complete proteome] [HAMAP]
Taxonomic identifier478009 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

Protein attributes

Sequence length311 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 – 311311Probable lipoyl synthase HAMAP-Rule MF_00206
PRO_1000099607

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 binding661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding701Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding731Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B0R7C4 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 8EE891416B65DB01

FASTA31134,830
        10         20         30         40         50         60 
MSSRRKPEWL KMRPPSGERF TDIKETLRDN DLHTVCEEAS CPNMGECWSG RDGPGTATFM 

        70         80         90        100        110        120 
LMGDRCSRGC NFCDVKTGGM EPLDPDEPAN VAESVAEIGL DYVVLTSVDR DDLDDQGAGH 

       130        140        150        160        170        180 
FARTIREIKE RDPSILVEVL IPDFQGEKSL VQKIIDAGPD VIAHNIETVA RRQVPVRDRR 

       190        200        210        220        230        240 
AGYEQSLSVL EYVTRESDIY TKTSIMLGVG EYDHEVYQTL GDLREAGVDV VTLGQYLQPS 

       250        260        270        280        290        300 
RSHLDVADYV HPQKFETWQR VAESEFGFLY CASGPMVRSS YKAGELFVDA VLREGKSVQE 

       310 
ARRNARRAAS E 

« Hide

References

[1]"Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1."
Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K., Ruepp A., Soppa J., Tittor J., Oesterhelt D.
Genomics 91:335-346(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29341 / DSM 671 / R1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM774415 Genomic DNA. Translation: CAP14643.1.
RefSeqYP_001689989.1. NC_010364.1.

3D structure databases

ProteinModelPortalB0R7C4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING478009.OE4111F.

Proteomic databases

PRIDEB0R7C4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP14643; CAP14643; OE_4111F.
GeneID5953295.
KEGGhsl:OE4111F.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMANVKKPEW.

Enzyme and pathway databases

BioCycHSAL478009:GJVF-1802-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_HALS3
AccessionPrimary (citable) accession number: B0R7C4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 44 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