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Q057Q7 (LIPA_BUCCC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:BCc_170
OrganismBuchnera aphidicola subsp. Cinara cedri (strain Cc) [Complete proteome] [HAMAP]
Taxonomic identifier372461 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length310 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 – 310310Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325237

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
Q057Q7 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: A0F66A351DB4118E

FASTA31035,523
        10         20         30         40         50         60 
MLKEKKDKEK NIYMIPKILK SSKSKSILKK PKWLKIKLPS NLKKINKIKK ILKKNFLHSV 

        70         80         90        100        110        120 
CEEANCPNLP ECFNNGTATF MILGSICTRK CPFCAVTKGR AQKIDKNEPK KILDIVIKLK 

       130        140        150        160        170        180 
LTYVVLTSVA RDDLKDGGAK HFSKCIYEIR KKKNIKVEIL VPDFRGKEKI ALKIFNKFPP 

       190        200        210        220        230        240 
DIFNHNIENV PRLYSLIRPG ADYIKSLNLL YQFKKICPNI PTKSGLMLGL GEKKKEIISV 

       250        260        270        280        290        300 
LKDLKSVGVS IVTIGQYLQP SKNHLLVQKY ITPKEFKNFE YIALSLGFSK VFCGPLVRSS 

       310 
YHADRQYLSF 

« Hide

References

[1]"A small microbial genome: the end of a long symbiotic relationship?"
Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M., Silva F.J., Moya A., Latorre A.
Science 314:312-313(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Cc.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000263 Genomic DNA. Translation: ABJ90642.1.
RefSeqYP_802735.1. NC_008513.1.

3D structure databases

ProteinModelPortalQ057Q7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING372461.BCc_170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ90642; ABJ90642; BCc_170.
GeneID4440781.
KEGGbcc:BCc_170.
PATRIC21246283. VBIBucAph7855_0162.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBAPH372461:GHAJ-170-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_BUCCC
AccessionPrimary (citable) accession number: Q057Q7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 55 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