Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A4G9C6 (LIPA_HERAR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:HEAR3003
OrganismHerminiimonas arsenicoxydans [Complete proteome] [HAMAP]
Taxonomic identifier204773 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeHerminiimonas

Protein attributes

Sequence length335 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 – 335335Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325264

Sites

Metal binding751Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding801Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding861Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1011Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1051Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1081Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A4G9C6 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: 40D04F1D07BE844D

FASTA33537,333
        10         20         30         40         50         60 
MTIDTNPESS TPSAPAYNPS EKQKGSAKTI RIPIKVVPME RLPKPDWIRV KAGSPSTRFY 

        70         80         90        100        110        120 
EIKDILRANN LVTVCEEASC PNIGECFGKG TATFMIMGDK CTRRCPFCDV GHGRPDPLDV 

       130        140        150        160        170        180 
NEPENLAKTI AALRLNYVVI TSVDRDDLRD GGAGHFAECI RRVRELSPNT RIEILVPDFR 

       190        200        210        220        230        240 
GRMDRALEIL NLAPPDVMNH NLETAPRLYK EARPGSDYAY SLNLLKRFKA LHPNTPTKSG 

       250        260        270        280        290        300 
IMVGLGETDE EVLQVMRDMR AHDVDMLTIG QYLMPSGDHL PVRRYVHPDT FKMYEEEAYK 

       310        320        330 
MGFAHAAVGA MVRSSYHADQ QAHGVTAGAS QLPHD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU207211 Genomic DNA. Translation: CAL63113.1.
RefSeqYP_001101234.1. NC_009138.1.

3D structure databases

ProteinModelPortalA4G9C6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204773.HEAR3003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL63113; CAL63113; HEAR3003.
GeneID4931922.
KEGGhar:HEAR3003.
PATRIC22115974. VBIHerArs17568_2844.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycHARS204773:GJCA-2894-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_HERAR
AccessionPrimary (citable) accession number: A4G9C6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: April 17, 2007
Last modified: February 19, 2014
This is version 54 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