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A1KKR0 (LIPA_MYCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:BCG_2234
OrganismMycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP]
Taxonomic identifier410289 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length311 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 Potential 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 – 311311Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000012235

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
A1KKR0 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 0594BBC9AB4A547A

FASTA31134,719
        10         20         30         40         50         60 
MSVAAEGRRL LRLEVRNAQT PIERKPPWIK TRARIGPEYT ELKNLVRREG LHTVCEEAGC 

        70         80         90        100        110        120 
PNIFECWEDR EATFLIGGDQ CTRRCDFCQI DTGKPAELDR DEPRRVADSV RTMGLRYATV 

       130        140        150        160        170        180 
TGVARDDLPD GGAWLYAATV RAIKELNPST GVELLIPDFN GEPTRLAEVF ESGPEVLAHN 

       190        200        210        220        230        240 
VETVPRIFKR IRPAFTYRRS LGVLTAARDA GLVTKSNLIL GLGETSDEVR TALGDLRDAG 

       250        260        270        280        290        300 
CDIVTITQYL RPSARHHPVE RWVKPEEFVQ FARFAEGLGF AGVLAGPLVR SSYRAGRLYE 

       310 
QARNSRALAS R 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM408590 Genomic DNA. Translation: CAL72222.1.
RefSeqYP_978323.1. NC_008769.1.

3D structure databases

ProteinModelPortalA1KKR0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING410289.BCG_2234.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL72222; CAL72222; BCG_2234.
GeneID4698687.
KEGGmbb:BCG_2234.
PATRIC18015354. VBIMycBov80988_2437.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAHPHIPTK.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycMBOV410289:GJW7-2261-MONOMER.
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_MYCBP
AccessionPrimary (citable) accession number: A1KKR0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 54 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