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C5Y9R0 (LIAS_SORBI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 32. 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
Ordered Locus Names:Sb06g018660
OrganismSorghum bicolor (Sorghum) (Sorghum vulgare) [Reference proteome]
Taxonomic identifier4558 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeSorghum

Protein attributes

Sequence length386 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
Reference proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   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 – ?Mitochondrion Potential
Chain? – 386Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128PRO_0000398856

Sites

Metal binding1131Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1181Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1241Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1481Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1511Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
C5Y9R0 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: A19F3845489C859C

FASTA38642,141
        10         20         30         40         50         60 
MHGRRHLAAS LTRALTQAPS RSISSTPSLL QTLDPSVPSP SPPPAAEPGR LAELRRRLQA 

        70         80         90        100        110        120 
DAPSLGDFAY SVEVGTRQRP LPKPKWMKET VPGGAKYAAI KAKLRELKLH TVCEEARCPN 

       130        140        150        160        170        180 
LGECWSGGET GTATATIMIL GDTCTRGCRF CNVKTSRTPP PPDPDEPSNV AQAIASWGLE 

       190        200        210        220        230        240 
YIVITSVDRD DLPDQGSGHF AETVQKLKAL KPEMLIEALV PDFRGDPSCV EKVATSGLHV 

       250        260        270        280        290        300 
FAHNIETVEE LQRNVRDYRA NFKQSIDVLK MAKEYAPPGT LTKTSIMLGC GETPDQVIST 

       310        320        330        340        350        360 
MEKVRAAGVD VITFGQYMRP SKRHMPVSEY VTPEAFEKYR ALGVEMGFRY VASGPMVRSS 

       370        380 
YKAGEFYIKA MIEADRSKAT TADSSA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM000765 Genomic DNA. Translation: EES12278.1.
RefSeqXP_002447950.1. XM_002447905.1.
UniGeneSbi.15755.

3D structure databases

ProteinModelPortalC5Y9R0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4558.Sb06g018660.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsSb06g018660.1; Sb06g018660.1; Sb06g018660.
GeneID8057459.
KEGGsbi:SORBI_06g018660.

Organism-specific databases

GrameneC5Y9R0.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.
OMAVQKYWTP.
ProtClustDBPLN02428.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
MF_03128. Lipoyl_synth_plantM.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
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_SORBI
AccessionPrimary (citable) accession number: C5Y9R0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 1, 2009
Last modified: March 19, 2014
This is version 32 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