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B8D7G6 (LIPA_BUCAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:BUAPTUC7_266
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7) [Complete proteome] [HAMAP]
Taxonomic identifier561501 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

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_1000124624

Sites

Metal binding651Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding701Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding761Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding911Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding951Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding981Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B8D7G6 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 117C1DDB49DBA9BF

FASTA32336,865
        10         20         30         40         50         60 
MKKNKDVLLK NKILKKLNII NIKNLDNIKE KLKKPDWIKI KIPVNTSRIY QIKNALRKNN 

        70         80         90        100        110        120 
LYSVCEEAHC PNLSECFNNG TATFMILGSI CTRNCPFCAV FHGRPNPVNV EEPQKLSDTI 

       130        140        150        160        170        180 
FDMGINYVVI TSVVRDDLYD GGAEHFVNCI KAIKNKNQVK IEILVPDFRG RIELILNIFN 

       190        200        210        220        230        240 
NALPDIFNHN IENVPRLYKK IRPGANYQRS LLLLESFKKK YCSVLTKSGL MLGLGEKDVE 

       250        260        270        280        290        300 
IIQVMKDLYS SGVTLLTVGQ YLQPSIHHLP VKRYIPLSEF ENIKKEALSI GFTNAFCGPF 

       310        320 
VRSSYHASFQ SHLPIKNNDI NNI 

« Hide

References

[1]"The dynamics and time scale of ongoing genomic erosion in symbiotic bacteria."
Moran N.A., McLaughlin H.J., Sorek R.
Science 323:379-382(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuc7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001158 Genomic DNA. Translation: ACL30081.1.
RefSeqYP_002468576.1. NC_011834.1.

3D structure databases

ProteinModelPortalB8D7G6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561501.BUAPTUC7_266.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL30081; ACL30081; BUAPTUC7_266.
GeneID7263118.
KEGGbau:BUAPTUC7_266.
PATRIC21248617. VBIBucAph26317_0263.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAVQKYWTP.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycBAPH561501:GHRN-265-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_BUCAT
AccessionPrimary (citable) accession number: B8D7G6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 39 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