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Q57390 (LIPA_PELCD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 102. 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
Synonyms:acoS
Ordered Locus Names:Pcar_0346
OrganismPelobacter carbinolicus (strain DSM 2380 / Gra Bd 1) [Complete proteome] [HAMAP]
Taxonomic identifier338963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

Protein attributes

Sequence length309 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 By similarity 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 – 309309Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000102333

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

Experimental info

Sequence conflict149 – 1513EGV → RRVY in AAA91878. Ref.1
Sequence conflict149 – 1513EGV → RRVY in AAA18918. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q57390 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 9EA24FB6E17AFAC7

FASTA30934,154
        10         20         30         40         50         60 
MDVGQKKRGA DKTALATTDE QGALSKPTWI RAKAPISPEV GRLTGILRDL HLHTVCEEAS 

        70         80         90        100        110        120 
CPNLGECFKR GTATFMIMGD VCTRRCPFCD VAHGRPAALD TEEPGHLADA IGAMKLKYVV 

       130        140        150        160        170        180 
ITSVTRDDLE DGGAAHFAQC IESIRKKTEG VKVEILVPDF RGHVDAALKN LGNCLPDVFN 

       190        200        210        220        230        240 
HNLETVPRLY AESRPGARYH ESLRLLQRFK ETYPGIPTKS GLMLGLGETD EEILEVMRDL 

       250        260        270        280        290        300 
RVHGCDMLTI GQYLRPSRHH LPVQRYVTPE QFEAFRVAGL KMGFSQVASG PLVRSSYHAD 


LQAKEVLHT 

« Hide

References

« Hide 'large scale' references
[1]"Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system."
Oppermann F.B., Steinbuechel A.
J. Bacteriol. 176:469-485(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Pelobacter carbinolicus DSM 2380."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2380 / Gra Bd 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L24124 Genomic DNA. Translation: AAA91878.1.
U01100 Unassigned DNA. Translation: AAA18918.1.
CP000142 Genomic DNA. Translation: ABA87606.1.
PIRE36953.
RefSeqYP_006716018.1. NC_007498.2.

3D structure databases

ProteinModelPortalQ57390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338963.Pcar_0346.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA87606; ABA87606; Pcar_0346.
GeneID3723479.
KEGGpca:Pcar_0346.
PATRIC22886614. VBIPelCar86875_0384.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPCAR338963:GKDU-394-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_PELCD
AccessionPrimary (citable) accession number: Q57390
Secondary accession number(s): Q3A7N8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 20, 2005
Last modified: February 19, 2014
This is version 102 of the entry and version 2 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