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A4HY57 (LIPA_LEIIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:LinJ19.0190, LinJ_19_0350
OrganismLeishmania infantum [Reference proteome]
Taxonomic identifier5671 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Protein attributes

Sequence length412 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
Reference proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrion

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 – ?Mitochondrion Potential
Chain? – 412Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398237

Sites

Metal binding1271Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1321Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1381Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1591Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A4HY57 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: CC21574ED808D2C6

FASTA41245,132
        10         20         30         40         50         60 
MCLTAAPSRV SPVAAAAAAA ADVAGSSEST VNLMADVDKK DPQYKQIFLE RFRKKLQSDK 

        70         80         90        100        110        120 
TGMNDLESFV ELPEGVAPSA ASIGPIKRGS EPLPPWLKLK VPKGMTHRPR FNRIRRSMRE 

       130        140        150        160        170        180 
KNLSTVCEEA KCPNIGECWG GSDDEGTATA TIMVMGSHCT RGCRFCSVLT SRRPPPLDPE 

       190        200        210        220        230        240 
EPEKVAAAVH EMGVDYIVMT MVDRDDLPDG GASHVCRCIH TIKEKNPALM LEALVGDFHG 

       250        260        270        280        290        300 
DLKLVEQLAV TPLSVYAHNI ECVERITPRV RDRRASYKQS LQTLEHVTKS TNGKMLTKSS 

       310        320        330        340        350        360 
IMLGLGEEEK EVRQTLRDLR TAGVSAVTLG QYLQPSRTRL KVSRYAHPKE FEMWEKEAMD 

       370        380        390        400        410 
MGFLYCASGP MVRSSYRAGE YYIKSILKQR QSAEGGKATA AATAANAGAA IA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FR796451 Genomic DNA. Translation: CAM67240.1.
RefSeqXP_001464998.1. XM_001464961.1.

3D structure databases

ProteinModelPortalA4HY57.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5671.LinJ19.0190.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5068408.
KEGGlif:LINJ_19_0350.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEWLRRPI.

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]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_LEIIN
AccessionPrimary (citable) accession number: A4HY57
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 1, 2007
Last modified: June 11, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways