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

A5E450 (LIPA_LODEL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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
ORF Names:LELG_04389
OrganismLodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome]
Taxonomic identifier379508 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeLodderomyces

Protein attributes

Sequence length432 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_03123

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_03123

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_03123

Subcellular location

Mitochondrion By similarity HAMAP-Rule MF_03123.

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? – 432Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398271

Sites

Metal binding1501Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1551Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1611Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1801Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1841Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1871Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A5E450 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 6371CA6B2C363D7C

FASTA43247,959
        10         20         30         40         50         60 
MLPRSINILK LRPTTQVTTT ALRALATEAK TTLGATPGST STSTSTSTAT TTTLESTSTS 

        70         80         90        100        110        120 
TSGDATETTI KETKSIKRKR TFFTDELNKG PSFDDFVSGK AKDMLEDPLE LARKDPNAKL 

       130        140        150        160        170        180 
PLWLKVPIPK GKSFHNVKND VRELKLSTVC EEAKCPNIGE CWGGKKSEAT ATIMLLGDTC 

       190        200        210        220        230        240 
TRGCRFCSVK TNRKPGKPDP MEPENTAEAI SRWGLGYVVL TTVDRDDLID GGANHLKETV 

       250        260        270        280        290        300 
QKIKFKAPQI LVEVLGGDFR GDLEMVKILA NSGLDVYAHN METVEALTPH IRDRRATYRQ 

       310        320        330        340        350        360 
SLAVLRTAKE TKPSLITKTS LMLGFGETDD QIRQTLKDLR EVGCDVVTFG QYMRPTKRHM 

       370        380        390        400        410        420 
KVVEYVTPEK FDYWRDVALE MGFLYVASGP LVRSSYKAGE AFIENVLKKR KHNVGESPRM 

       430 
LQEVKPSIFK RA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH981529 Genomic DNA. Translation: EDK46208.1.
RefSeqXP_001524417.1. XM_001524367.1.

3D structure databases

ProteinModelPortalA5E450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36914.A5E450.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5231419.
KEGGlel:LELG_04389.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.
OMAVQKYWTP.
OrthoDBEOG79KPR7.

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]
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_LODEL
AccessionPrimary (citable) accession number: A5E450
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways