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Q7W0K8 (LIPA_BORPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:BP0106
OrganismBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) [Reference proteome] [HAMAP]
Taxonomic identifier257313 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length333 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
Reference 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 – 333333Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000102292

Sites

Metal binding801Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding851Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding911Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1061Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1101Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1131Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7W0K8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: AE76F07F2342F024

FASTA33337,103
        10         20         30         40         50         60 
MSTLVESPVP SNDSQAAAPA AYDPTQKQKS QAKTARIPIK VVAAEKLKKP EWIRVRAAAP 

        70         80         90        100        110        120 
GSRFYDIKRI LREHNLHTVC EEASCPNIGE CFGKGTATFM IMGDKCTRRC PFCDVGHGRP 

       130        140        150        160        170        180 
DPLDTQEPEN LARTIAALKL SYVVITSVDR DDLRDGGAAH FVECIAKVRE YSPDTRIEVL 

       190        200        210        220        230        240 
VPDFRGRLDR ALHILNSGPP DVMNHNLETV PRLYKQARPG SDYAHSLKLL AEFKKLHPEV 

       250        260        270        280        290        300 
PTKSGLMLGL GETDEEILQV MRDMREHNVD MLTIGQYLQP SEHHLPVLRY VHPDTFAMFE 

       310        320        330 
REAYAMGFTH AAVGAMVRSS YHADQQAHAA GVN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX640411 Genomic DNA. Translation: CAE40486.1.
RefSeqNP_879009.1. NC_002929.2.

3D structure databases

ProteinModelPortalQ7W0K8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257313.BP0106.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE40486; CAE40486; BP0106.
GeneID2665325.
KEGGbpe:BP0106.
PATRIC21153200. VBIBorPer7866_0107.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAPEEPYNT.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycBPER257313:BP0106-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_BORPE
AccessionPrimary (citable) accession number: Q7W0K8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 73 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