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B6JDY1 (LIPA_OLICO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:OCAR_6091, OCA5_c19380
OrganismOligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5) [Complete proteome] [HAMAP]
Taxonomic identifier504832 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeOligotropha

Protein attributes

Sequence length322 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 – 322322Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000099616

Sites

Metal binding611Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding661Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding721Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding871Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding911Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding941Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B6JDY1 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: CFA0FCC2E8D60F11

FASTA32235,587
        10         20         30         40         50         60 
MVTLIDTISE RQVRPRHPEK AHRPDAISPP KPDWIRVRAP TSRGYANTRN IVKENGLVTV 

        70         80         90        100        110        120 
CEEAGCPNIG ECWDKKHATF MIMGDTCTRA CAFCNVRTGL PDGLDPDEPA HVALAVQKLG 

       130        140        150        160        170        180 
LAHVVITSVD RDDLADGGAA HFAATIAAIR ESCPTTTIEI LTPDFLRKEG ALEVVVAAKP 

       190        200        210        220        230        240 
DVFNHNLETV PSRYQSVRPG ARYFHSVRLL QRVKEIDPTI FTKSGIMVGL GEERHEVLQV 

       250        260        270        280        290        300 
MDDLRSADVD FLTIGQYLQP TLKHHAVMRY VTPEEFDGYE RIAFTKGFLM VSASPLTRSS 

       310        320 
HHAGEDFARL KAAREAKLQS AG 

« Hide

References

[1]"Genome sequence of the chemolithoautotrophic bacterium Oligotropha carboxidovorans OM5T."
Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.
J. Bacteriol. 190:5531-5532(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49405 / DSM 1227 / OM5.
[2]"Complete genome sequences of the chemolithoautotrophic Oligotropha carboxidovorans strains OM4 and OM5."
Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., Meyer O.
J. Bacteriol. 193:5043-5043(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49405 / DSM 1227 / OM5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001196 Genomic DNA. Translation: ACI93206.1.
CP002826 Genomic DNA. Translation: AEI06650.1.
RefSeqYP_002289071.1. NC_011386.1.
YP_004632891.1. NC_015684.1.

3D structure databases

ProteinModelPortalB6JDY1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING504832.OCAR_6091.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI93206; ACI93206; OCAR_6091.
AEI06650; AEI06650; OCA5_c19380.
GeneID10847070.
6992224.
KEGGoca:OCAR_6091.
ocg:OCA5_c19380.
PATRIC22806053. VBIOliCar134280_1979.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAPEEPYNT.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycOCAR504832:GJPZ-1938-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_OLICO
AccessionPrimary (citable) accession number: B6JDY1
Secondary accession number(s): F8BUZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 43 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