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

P61196 (LIPA_GEOSL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:GSU0380
OrganismGeobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) [Reference proteome] [HAMAP]
Taxonomic identifier243231 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length303 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 – 303303Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000102316

Sites

Metal binding351Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding401Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding461Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding611Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding651Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding681Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
P61196 [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: B63BE8FCEE0706C1

FASTA30332,887
        10         20         30         40         50         60 
MNIHRKPEWL RKKINPAAHG AMDELLGELR LHTVCREARC PNITECFRER QATFLILGAE 

        70         80         90        100        110        120 
CTRLCSFCNV TKGEPLPPDP DEPARVAQAV VRLSLAHVVI TSPTRDDLPD GGAGHYVATV 

       130        140        150        160        170        180 
ATIGRVAPAT VVELLIPDFL GSRAALADVV AAAPRIIGHN VETVPRLYAI RAGADYGRSL 

       190        200        210        220        230        240 
AVLRTLRELA PGCATKSGLM LGLGETEEEV LAVMADLRRV DCTYLSLGQY LAPSRFHHPV 

       250        260        270        280        290        300 
REFVLPETFD RLKELAEKMG FRHVESGPYV RSSYHAAGYG GGTRTDQPVA SGCLSDQEGV 


SAQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017180 Genomic DNA. Translation: AAR33712.1.
RefSeqNP_951439.1. NC_002939.5.

3D structure databases

ProteinModelPortalP61196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243231.GSU0380.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAR33712; AAR33712; GSU0380.
GeneID2686621.
KEGGgsu:GSU0380.
PATRIC22023504. VBIGeoSul17553_0378.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMACSFCNVT.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycGSUL243231:GH27-385-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.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_GEOSL
AccessionPrimary (citable) accession number: P61196
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: February 19, 2014
This is version 72 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