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B3PYS0 (LIPA_RHIE6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:RHECIAT_CH0002038
OrganismRhizobium etli (strain CIAT 652) [Complete proteome] [HAMAP]
Taxonomic identifier491916 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length323 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 – 323323Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000099624

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
B3PYS0 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: C14318A42EF873D7

FASTA32336,083
        10         20         30         40         50         60 
MVTILDTINP DAKRVRHPEK AHRPDTEVMR KPDWIRVKAP TSKGYAETRA IVKEHKLVTV 

        70         80         90        100        110        120 
CEEAGCPNIG ECWDKKHATF MIMGEICTRA CAFCNVATGK PNALDMAEPE NVAKAVKEMG 

       130        140        150        160        170        180 
LSHVVITSVD RDDLEDGGAE HFEKVIWAIR AASPATTIEI LTPDFLKKPG ALERVVAAKP 

       190        200        210        220        230        240 
DVFNHNMETV AGNYLTVRPG ARYFHSIRLL QRVKELDPTM FTKSGIMVGL GEERNEVLQL 

       250        260        270        280        290        300 
MDDLRTADVD FLTIGQYLQP TRKHHKVESF VTPDEFKSYE TVAYSKGFLM VASSPLTRSS 

       310        320 
HHAGDDFARL RAAREKKLLV AAE 

« Hide

References

[1]"Genome diversity and DNA divergence of Rhizobium etli."
Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J., Palacios R., Davila G.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIAT 652.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001074 Genomic DNA. Translation: ACE90999.1.
RefSeqYP_001978177.1. NC_010994.1.

3D structure databases

ProteinModelPortalB3PYS0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING491916.RHECIAT_CH0002038.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE90999; ACE90999; RHECIAT_CH0002038.
GeneID6400125.
KEGGrec:RHECIAT_CH0002038.
PATRIC23097547. VBIRhiEtl120572_2011.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRETL491916:GH4T-2037-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_RHIE6
AccessionPrimary (citable) accession number: B3PYS0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: February 19, 2014
This is version 44 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