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B9RX57 (LISC_RICCO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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, chloroplastic

EC=2.8.1.8
Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoate synthase, plastidial
Short name=LIP1p
Lipoic acid synthase
Gene names
Name:LIP1P
ORF Names:RCOM_0817880
OrganismRicinus communis (Castor bean) [Complete proteome]
Taxonomic identifier3988 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Protein attributes

Sequence length364 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_03129

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_03129

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_03129

Subcellular location

Plastidchloroplast Potential HAMAP-Rule MF_03129.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   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_componentchloroplast

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

Transit peptide1 – 7070Chloroplast Potential
Chain71 – 364294Lipoyl synthase, chloroplastic HAMAP-Rule MF_03129
PRO_0000398869

Sites

Metal binding951Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1001Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1061Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1261Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1301Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1331Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B9RX57 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: C3B55B75770C5DA9

FASTA36440,304
        10         20         30         40         50         60 
MEQTLFNPSI SMPKSFYHKH ITISSRIQCQ LSTNSPSSNT KTTTVTVPSK KTMGPYTGRD 

        70         80         90        100        110        120 
PNVKKPEWLR QRAPQGERFQ EVKHSLSSLK LNTVCEEAQC PNIGECWNGG GDGIATATIM 

       130        140        150        160        170        180 
LLGDTCTRGC RFCAVKTSRN PSPPDPLEPQ NTALAIASWG VDYIVLTSVD RDDLPDGGSG 

       190        200        210        220        230        240 
HFSETVQAMK KLKPEIMVEC LTSDFRGDLE AVETLVHSGL DVFAHNIETV KRLQRIVRDP 

       250        260        270        280        290        300 
RAGYEQSLSV LKHAKHSKEG MITKSSIMLG LGETDDELKE AMADLRAIDV DILTLGQYLQ 

       310        320        330        340        350        360 
PTPLHLTVKE YVTPEKFAFW KEYGESIGFR YVASGPMVRS SYRAGELFVK TMVKERSSNS 


AAKP 

« 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
EQ973826 Genomic DNA. Translation: EEF44086.1.
RefSeqXP_002518326.1. XM_002518280.1.

3D structure databases

ProteinModelPortalB9RX57.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8279195.
KEGGrcu:RCOM_0817880.

Phylogenomic databases

KOK03644.
ProtClustDBPLN02428.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
MF_03129. Lipoyl_synth_plantC.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027526. Lipoyl_synth_chlpt.
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 nameLISC_RICCO
AccessionPrimary (citable) accession number: B9RX57
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 24, 2009
Last modified: February 19, 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