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B9RW49 (LIAS_RICCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 31. 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, mitochondrial

EC=2.8.1.8
Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoic acid synthase
Gene names
Name:LIP1
ORF Names:RCOM_1176060
OrganismRicinus communis (Castor bean) [Complete proteome]
Taxonomic identifier3988 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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_03128

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_03128

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_03128

Subcellular location

Mitochondrion By similarity HAMAP-Rule MF_03128.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 348Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128PRO_0000398855

Sites

Metal binding1051Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1101Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1161Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1361Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1401Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1431Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B9RW49 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 05CAF5FBB2772DA3

FASTA34838,584
        10         20         30         40         50         60 
MFQSRFTILI RTLNSSKSRH FSSTIEPTKP QFPQTLAGLR ARLAAESPSL SEFSDLQSNN 

        70         80         90        100        110        120 
SYSVEVGTKK KPLPKPKWMR EAIPGGDKYV QIKKKLRELK LHTVCEEAKC PNLGECWSGG 

       130        140        150        160        170        180 
ETGTATATIM ILGDTCTRGC RFCNVKTSRT PPPPDPDEPA NVAEAIASWG LDYVVITSVD 

       190        200        210        220        230        240 
RDDLPDQGSN HFAQTVQKLK ALKPHMLIEA LVPDFRGDPG CVENVAKSGL DVFAHNIETV 

       250        260        270        280        290        300 
EDLQSVIRDH RANFKQSLDV LMMAKDHAPK GTLTKTSIML GCGETPEQVV KTMEKVRAAG 

       310        320        330        340 
VDVMTFGQYM RPSKRHMPVS EYVTPEAFEQ YRTXXLVSYV LFSLLISV 

« Hide

References

[1]"Draft genome sequence of the oilseed species Ricinus communis."
Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D., Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M., Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J., Rabinowicz P.D.
Nat. Biotechnol. 28:951-956(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Hale.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EQ973822 Genomic DNA. Translation: EEF44486.1.
RefSeqXP_002517968.1. XM_002517922.1.

3D structure databases

ProteinModelPortalB9RW49.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8262116.
KEGGrcu:RCOM_1176060.

Phylogenomic databases

KOK03644.

Enzyme and pathway databases

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 nameLIAS_RICCO
AccessionPrimary (citable) accession number: B9RW49
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways