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Q2U4H2 (LIPA_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:AO090020000344
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

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)
   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 – 3232Mitochondrion Potential
Chain33 – 415383Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398256

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
Q2U4H2 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: D70539BCDC1DF0FB

FASTA41545,818
        10         20         30         40         50         60 
MAASTNRLRF LYSSARTVPQ TGSITPISRR TYATTEPSPS ATGAPATARK RTNFTDKLNA 

        70         80         90        100        110        120 
GPSFADFVSG GEDNAPLEPS EAYALKTAMV GPAGRKKEMT RLPSWLKTPI PDSKNYQRLK 

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

       190        200        210        220        230        240 
LDPHEPENTA EAISRWSLGY VVLTSVDRDD LADGGARHFA ETVIKIKQKK PSMLVECLTG 

       250        260        270        280        290        300 
DYLGDLEMVK LVARSGLDVY AHNVETVEAL TPFVRDRRAT FQQSLRVLEA AKQARPDLIT 

       310        320        330        340        350        360 
KTSLMLGFGE TEEQLWDALR QLRSVGVDVV TFGQYMRPTK RHMPVHEYVT PDQFELWRQR 

       370        380        390        400        410 
ALDMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRAAGTAG ESVTDSKAAV DEATR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007167 Genomic DNA. Translation: BAE63543.1.
RefSeqXP_001824676.1. XM_001824624.2.

3D structure databases

ProteinModelPortalQ2U4H2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00006700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00006831; CADAORAP00006700; CADAORAG00006831.
GeneID5996762.
KEGGaor:AOR_1_608084.

Phylogenomic databases

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

Entry information

Entry nameLIPA_ASPOR
AccessionPrimary (citable) accession number: Q2U4H2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 54 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