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Q7NFJ9 (LIPA2_GLOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. 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 2

EC=2.8.1.8
Alternative name(s):
Lip-syn 2
Lipoate synthase 2
Lipoic acid synthase 2
Sulfur insertion protein lipA2
Gene names
Name:lipA2
Ordered Locus Names:gll3526
OrganismGloeobacter violaceus (strain PCC 7421) [Reference proteome] [HAMAP]
Taxonomic identifier251221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter

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
Reference 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 2 HAMAP-Rule MF_00206
PRO_0000102317

Sites

Metal binding431Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding481Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding541Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding691Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding731Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding761Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NFJ9 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 37A1CD474D675519

FASTA28931,777
        10         20         30         40         50         60 
MLAMSHQTAS SRLPEWARRT IGTASQVSTV EKIVKQRSLH TICEEGRCPN RAECYAQKTA 

        70         80         90        100        110        120 
TFLLMGPVCT RACGFCQVAG GKALPLDPQE PEKVAEAVAL LGLKYVVLTS VARDDLPDQG 

       130        140        150        160        170        180 
AGWFVRTMES IRARNCAVEI EVLTPDFRGE EACIATVVAA RPVCFNHNIE TVRRLQSYAR 

       190        200        210        220        230        240 
RAATYARSLA VLAAVKRLDA EIFTKSGLML GHGETREEVL ETLLDLRKVG CDRVTLGQYL 

       250        260        270        280 
QPSKDHLPVH KYWTPAEFAE LGAVARDLGF AHVRSGPLVR SSYHAGEPE 

« Hide

References

[1]"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.
DNA Res. 10:137-145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000045 Genomic DNA. Translation: BAC91467.1.
RefSeqNP_926472.1. NC_005125.1.

3D structure databases

ProteinModelPortalQ7NFJ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING251221.gll3526.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC91467; BAC91467; BAC91467.
GeneID2601930.
KEGGgvi:gll3526.
PATRIC22046543. VBIGloVio86258_3559.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEWLRRPI.
OrthoDBEOG6038ZS.
PhylomeDBQ7NFJ9.

Enzyme and pathway databases

BioCycGVIO251221:GH9A-3573-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 nameLIPA2_GLOVI
AccessionPrimary (citable) accession number: Q7NFJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 74 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