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A3GGJ5 (LIPA_PICST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 53. 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:PICST_86231
OrganismScheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis) [Complete proteome]
Taxonomic identifier322104 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeScheffersomyces

Protein attributes

Sequence length398 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 – 398366Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398283

Sites

Metal binding1171Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1221Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1281Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1471Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1511Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1541Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A3GGJ5 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: A10E1466D9D973B5

FASTA39844,638
        10         20         30         40         50         60 
MIALRVHNTR VVSRSLTVWT RPSPTLTLSR SLATESDALD KPKTRRRKTV FTDALNSGPS 

        70         80         90        100        110        120 
FDDFVSGKAS EIMDPLEAAR KDPNQRLPSW LKVPIPKGKS YHNVKKDVRE LKLATVCEEA 

       130        140        150        160        170        180 
KCPNIGECWG GKKSEATATI MLLGDTCTRG CRFCSVKTNR NPAKPDPMEP ENTAEAISRW 

       190        200        210        220        230        240 
GLGYVVLTTV DRDDLADGGA HHLAETVMKI KQKAPQILVE VLGGDFRGDL DMATVLAKSG 

       250        260        270        280        290        300 
LDVYAHNLET VEALTPFVRD RRATYRQSLS VLQRAKETKS SLVTKTSLML GLGETDEQIL 

       310        320        330        340        350        360 
QTLKDLREIN CDVVTFGQYM RPTKRHMKVV EYVTPEKFDY WRDTALEMGF LYVASGPLVR 

       370        380        390 
SSYKAGEAFI ENVIRKRRHN VGEAPRLAQE IQPKIFRE 

« Hide

References

[1]"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis."
Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.
Nat. Biotechnol. 25:319-326(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAVQ01000001 Genomic DNA. Translation: EAZ63945.2.
RefSeqXP_001387968.2. XM_001387931.1.

3D structure databases

ProteinModelPortalA3GGJ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4924.PICST_86231.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4851394.
KEGGpic:PICST_86231.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAHPHIPTK.
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_PICST
AccessionPrimary (citable) accession number: A3GGJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 16, 2009
Last modified: June 11, 2014
This is version 53 of the entry and version 2 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