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B6QSZ4 (LIPA_PENMQ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 30. 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:PMAA_003450
OrganismPenicillium marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) [Complete proteome]
Taxonomic identifier441960 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces

Protein attributes

Sequence length425 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 – 3333Mitochondrion Potential
Chain34 – 425392Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398279

Sites

Metal binding1421Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1471Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1531Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1731Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1771Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1801Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B6QSZ4 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: E1A082491BFA6990

FASTA42546,515
        10         20         30         40         50         60 
MAASSTRLRC LYASSSTWKT SPSQSLISLS RRYATTSSAP PTPSDESSST LPKRRKTTTF 

        70         80         90        100        110        120 
KDKLNAGPSF ADFVSGNGDS NNAPLDASEA YALETVMIPG PAGRGKKEHT RLPSWLKTPI 

       130        140        150        160        170        180 
PDSTNYKRIK KDLRGLKLNT VCEEARCPNI SDCWGGSDKS AATATIMLMG DSCTRGCRFC 

       190        200        210        220        230        240 
SVKTLRTPGP LDPHEPENTA EALSRWGLGY VVLTSVDRDD LSDGGAHHFA ETVIKIKQKA 

       250        260        270        280        290        300 
PGILVECLTG DFAGDFDMVA LVAKSGLDVY AHNVETVEAL TPHVRDRRAT FQQSLRVLEA 

       310        320        330        340        350        360 
AKRAKPSLIT KTSMMLGFGE TEDQMWDALR QLRASNVDVV TFGQYMRPTK RHMAVHEYVT 

       370        380        390        400        410        420 
PDKFELWRQR ALEMGFLYVA SGPLVRSSYK AGEAFIENVL KKRRGVGNTP GAEVTTEVPV 


DALAK 

« Hide

References

[1]"The genome sequence of Penicillium marneffei strain ATCC 18224."
Fedorova N.D., Joardar V.S., Maiti R., Schobel S., Amedeo P., Galens K., Inman J.M., White O.R., Whitty B.R., Wortman J.R., Nierman W.C.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 18224 / CBS 334.59 / QM 7333.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS995905 Genomic DNA. Translation: EEA19557.1.
RefSeqXP_002152494.1. XM_002152458.1.

3D structure databases

ProteinModelPortalB6QSZ4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7029911.

Phylogenomic databases

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_PENMQ
AccessionPrimary (citable) accession number: B6QSZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 16, 2008
Last modified: June 11, 2014
This is version 30 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