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Q7U4D9 (LIPA1_SYNPX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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 1

EC=2.8.1.8
Alternative name(s):
Lip-syn 1
Lipoate synthase 1
Lipoic acid synthase 1
Sulfur insertion protein lipA1
Gene names
Name:lipA1
Synonyms:lipA
Ordered Locus Names:SYNW2130
OrganismSynechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]
Taxonomic identifier84588 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length289 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 – 289289Lipoyl synthase 1 HAMAP-Rule MF_00206
PRO_0000102369

Sites

Metal binding331Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding381Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding441Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding591Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7U4D9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: B9F35FA576A99D8A

FASTA28932,291
        10         20         30         40         50         60 
MLKPEWLRVK APQRERIGAV ADLLLDLNLN TVCQEASCPN IGECFAGGTA TFLIMGPGCT 

        70         80         90        100        110        120 
RACPYCDIDF DKSVRELDPT EPERLGEAVA RLGLKHVVIT SVNRDDLPDG GATQFVACIE 

       130        140        150        160        170        180 
QVKQRSPLTT IELLIPDFCG NWDALATVMA AAPHVLNHNI ETVPRMYRLA RPQGIYERSL 

       190        200        210        220        230        240 
ELLQRVRDDW PRAYSKSGLM VGLGETDDEV IDVLRDLRTH RVDIVTIGQY LSPGPKHLAV 

       250        260        270        280 
DRFVTPEQFD TYRRIGEEEL GFLQVVSTPL TRSSYHAGEV QRLMASHPR 

« Hide

References

[1]"The genome of a motile marine Synechococcus."
Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.
Nature 424:1037-1042(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WH8102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX569694 Genomic DNA. Translation: CAE08645.1.
RefSeqNP_898221.1. NC_005070.1.

3D structure databases

ProteinModelPortalQ7U4D9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING84588.SYNW2130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE08645; CAE08645; SYNW2130.
GeneID1730610.
KEGGsyw:SYNW2130.
PATRIC23835989. VBISynSp27240_2271.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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 nameLIPA1_SYNPX
AccessionPrimary (citable) accession number: Q7U4D9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 73 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