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C5XKZ1 (LISC_SORBI) 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, 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
Ordered Locus Names:Sb03g035760
OrganismSorghum bicolor (Sorghum) (Sorghum vulgare) [Reference proteome]
Taxonomic identifier4558 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeSorghum

Protein attributes

Sequence length368 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 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
Reference 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 – ?Chloroplast Potential
Chain? – 368Lipoyl synthase, chloroplastic HAMAP-Rule MF_03129PRO_0000398870

Sites

Metal binding941Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding991Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1051Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1311Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1351Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1381Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
C5XKZ1 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: B63753E5085C935C

FASTA36839,528
        10         20         30         40         50         60 
MQSSLARPLR PPVLAGCGGR RGHGAPRGSV SVARCRAEAA PPTVGTASRA PAGPYTGRDP 

        70         80         90        100        110        120 
EVKKPAWLRQ RAAQGDKYAR LRESIGELKL NTVCVEAQCP NIGECWNGGG GAGGEGDGIA 

       130        140        150        160        170        180 
TATIMVLGDT CTRGCRFCAV KTSNKPPPPD PLEPLNTALA VASWGVDYVV LTSVDRDDLP 

       190        200        210        220        230        240 
DGGSSHFAQT VRALKELKPG ILVECLTSDF RGDLEAVSSL ANSGLDVYAH NIETVRSLQR 

       250        260        270        280        290        300 
IVRDPRAGYD QSLAVLKHAK DCREGMITKS SIMLGLGETD EEVKQAMIDL RAIGVDILTL 

       310        320        330        340        350        360 
GQYLQPTERH LTVREYVTPE KFQFWKEYGE SVGFRYVASG PLVRSSYRAG ELFVQNLVRN 


NKTGSSSS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM000762 Genomic DNA. Translation: EES01528.1.
RefSeqXP_002456408.1. XM_002456363.1.

3D structure databases

ProteinModelPortalC5XKZ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4558.Sb03g035760.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsSb03g035760.1; Sb03g035760.1; Sb03g035760.
GeneID8072124.
KEGGsbi:SORBI_03g035760.

Organism-specific databases

GrameneC5XKZ1.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.
OMACKEGMIT.

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_SORBI
AccessionPrimary (citable) accession number: C5XKZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 1, 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