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Q1GTM7 (LIPA_SPHAL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:Sala_1281
OrganismSphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) (Sphingomonas alaskensis) [Complete proteome] [HAMAP]
Taxonomic identifier317655 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingopyxis

Protein attributes

Sequence length311 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 – 311311Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325312

Sites

Metal binding471Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding521Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding581Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding731Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding771Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding801Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GTM7 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: D2C84F0C955C0725

FASTA31134,501
        10         20         30         40         50         60 
MNAPASPAAS PSQRARKPDW IRVKAPTSPG YAETRKLMRE LNLHTVCEEA ACPNIGECWT 

        70         80         90        100        110        120 
KKHATVMILG DTCTRACAFC NVKTGMPRPV DLLEPEHTAI AAAKMGLSHI VITSVDRDDL 

       130        140        150        160        170        180 
PDGGASQFVK VINALRRETP QTTIEILTPD FRNKPESAVA AIVDARPDVY NHNLETVPRL 

       190        200        210        220        230        240 
YPTIRPGARY YASLRLLESV KRRDPSIFTK SGIMLGLGEE RMEVHQVMDD MRSADIDFMT 

       250        260        270        280        290        300 
MGQYLQPTPK HAKVIDFVTP QAFDAYAQIA RAKGFLQVAS SPLTRSSYHA GDDFEHMRAA 

       310 
REAQLARVRA D 

« Hide

References

[1]"Complete sequence of chromosome of Sphingopyxis alaskensis RB2256."
US DOE Joint Genome Institute
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., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Chertkov O., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Cavicchioli R., Robb F., Ertan H., Schut F., Ting L.M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13593 / LMG 18877 / RB2256.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000356 Genomic DNA. Translation: ABF52995.1.
RefSeqYP_616328.1. NC_008048.1.

3D structure databases

ProteinModelPortalQ1GTM7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING317655.Sala_1281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF52995; ABF52995; Sala_1281.
GeneID4082532.
KEGGsal:Sala_1281.
PATRIC23691772. VBISphAla23391_1324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycSALA317655:GHHY-1289-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_SPHAL
AccessionPrimary (citable) accession number: Q1GTM7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 59 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