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

A0LTD9 (LIPA_ACIC1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:Acel_0926
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus

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_1000012178

Sites

Metal binding561Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding611Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding671Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding821Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding861Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding891Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LTD9 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 852E2BEBF2AAFCCE

FASTA32336,163
        10         20         30         40         50         60 
MTAVTPDGRK LLRIEARNAQ VPIERKPAWI RTRARMGPQY HALKELVRRE GLHTVCEEAG 

        70         80         90        100        110        120 
CPNIFECWED REATFLIGGD TCSRNCSFCQ ISSGRPQPLD RDEPRRVAES VARMGLRYAT 

       130        140        150        160        170        180 
VTGVTRDDLD DEGAWLYAQT VREIHHAVPG CGVELLTPDF HGRPELLDEV FSARPEVFAH 

       190        200        210        220        230        240 
NIETVPRIFK SIRPGFRYER SLDVLRAAHD AGLVTKSNLI LGLGETRQEI RAALADLRSA 

       250        260        270        280        290        300 
GCDLVTITQY LRPSIRHHPV VRWVEPAEFE ELAAEARELG FAGVMSGPLV RSSYRAGRLY 

       310        320 
RAAIASRTDR RTDGATTQAP QTP 

« Hide

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43068 / 11B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000481 Genomic DNA. Translation: ABK52699.1.
RefSeqYP_872685.1. NC_008578.1.

3D structure databases

ProteinModelPortalA0LTD9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351607.Acel_0926.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK52699; ABK52699; Acel_0926.
GeneID4485920.
KEGGace:Acel_0926.
PATRIC20672290. VBIAciCel132453_0983.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycACEL351607:GIXW-949-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_ACIC1
AccessionPrimary (citable) accession number: A0LTD9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: February 19, 2014
This is version 53 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