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B9KSE2 (LIPA_RHOSK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:RSKD131_1089
OrganismRhodobacter sphaeroides (strain KD131 / KCTC 12085) [Complete proteome] [HAMAP]
Taxonomic identifier557760 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length320 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 – 320320Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000124643

Sites

Metal binding601Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding651Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding711Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding861Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding901Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding931Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B9KSE2 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 0BF64485962BE698

FASTA32035,492
        10         20         30         40         50         60 
MIGKLVRDLK IPDQRHPEKA HRPDNVQPKK PSWIRVKAPT SEGYKETRDI IRGQKLATVC 

        70         80         90        100        110        120 
EEAGCPNVGE CWSQGHATMM IMGEICTRGC SFCNVATGRP QALDAFEPGR VAHAVSQLGL 

       130        140        150        160        170        180 
KHVVVTSVDR DDLEDGGAEH FAQTIRAIRH RAPATTIEVL VPDFLKCGPS ALETVVAARP 

       190        200        210        220        230        240 
DVFNHNLETV PGLYPEVRPG ARYFHSLRLL QRAKELDPSI FTKSGIMVGL GEDRQGVLQV 

       250        260        270        280        290        300 
MDDMRSAEVD FLTIGQYLQP TPKHHRVDRF VTPEEFAGYE KAAYGKGFLM VSATPLTRSS 

       310        320 
YHAGDDFARL RDARQKRLGA 

« Hide

References

[1]"Complete genome sequence of Rhodobacter sphaeroides KD131."
Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.
J. Bacteriol. 191:1118-1119(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KD131 / KCTC 12085.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001150 Genomic DNA. Translation: ACM00949.1.
RefSeqYP_002525450.1. NC_011963.1.

3D structure databases

ProteinModelPortalB9KSE2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557760.RSKD131_1089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM00949; ACM00949; RSKD131_1089.
GeneID7360504.
KEGGrsk:RSKD131_1089.
PATRIC23181277. VBIRhoSph125910_2502.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRSPH557760:GH1P-1099-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_RHOSK
AccessionPrimary (citable) accession number: B9KSE2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 40 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