Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A5CB81 (LIAS_VITVI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 41. 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:VITISV_021769
OrganismVitis vinifera (Grape)
Taxonomic identifier29760 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsVitalesVitaceaeVitis

Protein attributes

Sequence length393 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
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? – 393Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128PRO_0000398857

Sites

Metal binding1151Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1201Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1261Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1461Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1501Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1531Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A5CB81 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 18F30ED79ECD49A3

FASTA39343,477
        10         20         30         40         50         60 
MYTRLSSLAL RHHRHNHNNS VLLLSSLISL RHCSSPPTNP EPPQTLASLR HRLAVESPSL 

        70         80         90        100        110        120 
SDFVRLQTSD DYSVEVGTKK KPLSKPKWMK ESIPGGAKYT QIKKKLRQLN LHTVCEEARC 

       130        140        150        160        170        180 
PNMGECWSGG ETGTATATIM ILGDTCTRGC RFCNVKTSRT PPPPDPDEPS KVAEAIASWG 

       190        200        210        220        230        240 
LDYVVITSVD RDDLPDQGSG HFAETVQKLK ILKPNMLIEA LVPDFRGDPG CVEKVSKSGL 

       250        260        270        280        290        300 
DVFAHNIETV EELQSAVRDH RANFKQSLEV LKLAKEYADA GTLTKTSIML GCGETPDQVV 

       310        320        330        340        350        360 
RTMEKVRAAG VDVMTFGQYM RPSKRHMPVS EYITPEAFEK YRILGMDMGF RYVASGPMVR 

       370        380        390 
SSYKAGEFYI KSMIDADRAM SWASSSPSPL PAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM488835 Genomic DNA. Translation: CAN73265.1.
RefSeqXP_002266132.2. XM_002266096.2.
UniGeneVvi.610.

3D structure databases

ProteinModelPortalA5CB81.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING29760.GSVIVG00003955001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100251365.
KEGGvvi:100251365.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.

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_VITVI
AccessionPrimary (citable) accession number: A5CB81
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 41 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