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O32962 (LIPA_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. 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

EC=2.8.1.8
Alternative name(s):
Lip-syn
Short name=LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA
Gene names
Name:lipA
Ordered Locus Names:ML0858
ORF Names:MLCB22.20
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
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_00206

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_00206

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_00206

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00206.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   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_componentcytoplasm

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

Chain1 – 314314Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000102324

Sites

Metal binding551Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding601Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding661Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding811Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding851Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding881Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
O32962 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 6B998A6D54D846A4

FASTA31435,120
        10         20         30         40         50         60 
MTVAPEDCRL LRLEVRNAQT PIERKPPWIK TRARMGPEYT ALKNLVRRVA LHTVCEEAGC 

        70         80         90        100        110        120 
PNIFECWEDR EATFLIGGDQ CTRRCDFCQI DTGKPAALDR DEPRRVAESV QTMGLRYTTV 

       130        140        150        160        170        180 
TGVARDDLPD GGAWLYATTV RAIKELNPST GVELLIPDFN GQPARLAEVF DSRPQVLAHN 

       190        200        210        220        230        240 
VETVPRIFKR IRPAFTYQRS LDVLTAAREA GLVTKSNLIL GLGETADEVR TALADLRKTG 

       250        260        270        280        290        300 
CDIVTITQYL RPSMRHHPVE RWVRPEEFVE YTQYAEGLGF SGVLGGPLVR SSYRAGRLYE 

       310 
QAAGTRTVGT SVSR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z98741 Genomic DNA. Translation: CAB11385.1.
AL583920 Genomic DNA. Translation: CAC31239.1.
PIRT44895.
RefSeqNP_301646.1. NC_002677.1.

3D structure databases

ProteinModelPortalO32962.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML0858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC31239; CAC31239; CAC31239.
GeneID909865.
KEGGmle:ML0858.
PATRIC18053278. VBIMycLep78757_1584.

Organism-specific databases

LepromaML0858.
CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

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_MYCLE
AccessionPrimary (citable) accession number: O32962
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways