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

A1D855 (LIPA_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 49. 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:NFIA_070700
OrganismNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]
Taxonomic identifier331117 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya

Protein attributes

Sequence length415 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 Potential 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)
   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 – 3232Mitochondrion Potential
Chain33 – 415383Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398274

Sites

Metal binding1321Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1431Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1701Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A1D855 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 21E2ED4445F67DB8

FASTA41545,584
        10         20         30         40         50         60 
MAVSTSHFRS LCASSRSLSR TGIVAPISCR GYATTEPSPS ATSTTTTTTA RRRTTFKDKL 

        70         80         90        100        110        120 
NAGPSFADFV GNDNAPLDPS EAYALKTALV GPAGRKKEMT RLPSWLKTPI PDSKNYQRLK 

       130        140        150        160        170        180 
KDLRGLNLHT VCEEARCPNI SDCWGGSDKS AATATIMLMG DTCTRGCRFC SVKTSRTPSP 

       190        200        210        220        230        240 
LDPHEPENTA EAISRWGLGY VVLTSVDRDD LADGGARHFA ETVMKIKQKA PSILVECLTG 

       250        260        270        280        290        300 
DYAGDLEMVK LVARSGLDVY AHNVETVEAL TPQVRDRRAN FQQSIRVLEA AKNAQPSLIT 

       310        320        330        340        350        360 
KTSLMLGLGE TDEQLWDALR QLRVVNVDVV TFGQYMRPTK RHMAVHEYVT PDRFELWRQR 

       370        380        390        400        410 
ALDMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRAASGST ETVGVRPVAV DEVTR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027690 Genomic DNA. Translation: EAW21899.1.
RefSeqXP_001263796.1. XM_001263795.1.

3D structure databases

ProteinModelPortalA1D855.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36630.CADNFIAP00005581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADNFIAT00005738; CADNFIAP00005581; CADNFIAG00005738.
GeneID4590442.
KEGGnfi:NFIA_070700.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAPEEPYNT.
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]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_NEOFI
AccessionPrimary (citable) accession number: A1D855
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 49 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