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Q6FPY0 (LIPA_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. 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
Ordered Locus Names:CAGL0I10923g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces

Protein attributes

Sequence length388 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 – 1818Mitochondrion Potential
Chain19 – 388370Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398260

Sites

Metal binding1201Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1251Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1311Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1511Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1551Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1581Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FPY0 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 457598F13CF7B740

FASTA38843,401
        10         20         30         40         50         60 
MRLTTVQRRF LVSTKAKVSG ASISSTANTG SASAGAPNGQ TRRRRRITEF KDALNLGPSF 

        70         80         90        100        110        120 
EDFVSGRAAG FTVVDPLEQM RQDREEYKKL PKWLKVPIPK GVNYHKLKKD VKELKLSTVC 

       130        140        150        160        170        180 
EEARCPNIGE CWGGKDKSKA TATIMLLGDT CTRGCRFCSV KTNRNPAKPD PTEPENTAEA 

       190        200        210        220        230        240 
ISRWGLGYVV LTTVDRDDLP DGGAHHLAET VIKIKQKAPK TLVEALTGDF LGNLEMVDVM 

       250        260        270        280        290        300 
AKSGLDVYAH NLETVEALTP HVRDRRAGYR QSLNVLKRAK ETVPSLITKT SVMLGLGETD 

       310        320        330        340        350        360 
DQIIQTMQDL RAINCDVITF GQYMRPTKRH MKVVEYVRPE KFDYWKDKAK EMGFLYCASG 

       370        380 
PLVRSSYKAG EAFIENVLNK RKQDNKRI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR380955 Genomic DNA. Translation: CAG60659.1.
RefSeqXP_447714.1. XM_447714.1.

3D structure databases

ProteinModelPortalQ6FPY0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2889354.
KEGGcgr:CAGL0I10923g.

Phylogenomic databases

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_CANGA
AccessionPrimary (citable) accession number: Q6FPY0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 19, 2004
Last modified: June 11, 2014
This is version 71 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