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

Q1D4N0 (LIPA_MYXXD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:MXAN_4218
OrganismMyxococcus xanthus (strain DK 1622) [Complete proteome] [HAMAP]
Taxonomic identifier246197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeMyxococcus

Protein attributes

Sequence length298 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.

Sequence caution

The sequence ABF91066.1 differs from that shown. Reason: Erroneous initiation.

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 – 298298Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325279

Sites

Metal binding371Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding421Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding481Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding701Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1D4N0 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: C479F810831600C3

FASTA29833,737
        10         20         30         40         50         60 
MTETTRKPEW LKVRLPHGEG YERVKAIVKR TKLATVCEEA RCPNIAECWG GGTATVMLMG 

        70         80         90        100        110        120 
EVCTRACRFC HVKVGAPPPL DPMEPIHLAQ AVKEMDLEYI VVTSVNRDDR PDGGASHFAS 

       130        140        150        160        170        180 
AIRELRRESP RTIVEVLIPD FKGVEKDLTT VAEAKPHVVA HNVETVERLT PTVRDRRAKY 

       190        200        210        220        230        240 
HQSLRVLEYL KNRPEGLYTK TSVMVGLGET DAELEQTFKD LRDVGVDVLT LGQYLQPSQY 

       250        260        270        280        290 
HLRVERFVTP AQFEAYKTLA ESYGFLYVAS GPLVRSSYRA AEFFMKGLME RERLERLG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000113 Genomic DNA. Translation: ABF91066.1. Different initiation.
RefSeqYP_632393.1. NC_008095.1.

3D structure databases

ProteinModelPortalQ1D4N0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246197.MXAN_4218.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF91066; ABF91066; MXAN_4218.
GeneID4105746.
KEGGmxa:MXAN_4218.
PATRIC22650995. VBIMyxXan43560_4160.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycMXAN246197:GIWU-4182-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_MYXXD
AccessionPrimary (citable) accession number: Q1D4N0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: February 19, 2014
This is version 60 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