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

B5RUV1 (LIPA_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:DEHA2G18854g
OrganismDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier284592 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces

Protein attributes

Sequence length395 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 – 1414Mitochondrion Potential
Chain15 – 395381Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398266

Sites

Metal binding1121Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1171Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1231Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1421Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1461Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1491Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B5RUV1 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: 0E99DCBC39A30A45

FASTA39544,126
        10         20         30         40         50         60 
MISLRSISRS PAVQPARIYR TLATADTSGI NEQAKPKTKR KKTVFSDSLN KGPSFEDFVN 

        70         80         90        100        110        120 
GKAADMLVDP LEAARQDPNQ RLPKWLKVPI PKGKSFNNLK NDVRELKLAT VCEEAKCPNI 

       130        140        150        160        170        180 
GECWGGKKSE ATATIMLMGD TCTRGCRFCS VKTSRAPAKP DPMEPENTAE AISRWGLGYV 

       190        200        210        220        230        240 
VLTTVDRDDL VDGGANHLAE TVRKIKEKAP QILVEVLGGD FRGDLDMAAI LARSGLDVYA 

       250        260        270        280        290        300 
HNIETVEALT PYVRDRRATY RQSLSILNKA KETKPSLVTK TSLMLGFGET DEQIMQTLKD 

       310        320        330        340        350        360 
LREIKCDVVT FGQYMRPTKR HMKVVDYVKP EKFDYWRDTA LQMGFLYVAS GPLVRSSYKA 

       370        380        390 
GEAFIENVIR KRRHNVGETP RLAQEVNPKI ISQSI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382139 Genomic DNA. Translation: CAR65995.1.
RefSeqXP_002770663.1. XM_002770617.1.

3D structure databases

ProteinModelPortalB5RUV1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4959.B5RUV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8999246.
KEGGdha:DEHA2G18854g.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEEYVTPE.
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_DEBHA
AccessionPrimary (citable) accession number: B5RUV1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: November 4, 2008
Last modified: February 19, 2014
This is version 39 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