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

Q5XIH4 (LIAS_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. 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, mitochondrial

EC=2.8.1.8
Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoic acid synthase
Gene names
Name:Lias
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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_03123

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_03123

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_03123

Subcellular location

Mitochondrion By similarity HAMAP-Rule MF_03123.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Potential
Chain27 – 373347Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000332311

Sites

Metal binding1051Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1101Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1161Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1361Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1401Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1431Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5XIH4 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: F2108A035F9C7B14

FASTA37341,874
        10         20         30         40         50         60 
MALRCWDAAR SLGSRIFGRY ACSVRALSSL PDEKKKFLHN GPDLQDFVSG DLADKSTWDD 

        70         80         90        100        110        120 
YKGNLKRQKG ERLRLPPWLK TKIPMGKNYN KLKNTLRNLN LHTVCEEARC PNIGECWGGG 

       130        140        150        160        170        180 
EYATATATIM LMGDTCTRGC RFCSVKTARN PPPLDPSEPD NTARAIAEWG LDYVVLTSVD 

       190        200        210        220        230        240 
RDDVVDGGAE HIAKTVSCLK ERNPKILVEC LTPDFRGDLR AVEKVALSGL DVYAHNVETV 

       250        260        270        280        290        300 
PELQRKVRDP RANFDQSLRV LKHAKEVQPD VVSKTSIMLG LGETDEQVYA TMKALRAADV 

       310        320        330        340        350        360 
DCLTLGQYMQ PTKRHLKVEE YVTPEKFKYW EEVGNELGFH YTASGPLVRS SYKAGEFFLK 

       370 
NLVAKRKTKV SKV 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC083708 mRNA. Translation: AAH83708.1.
RefSeqNP_001012037.1. NM_001012037.1.
UniGeneRn.25547.

3D structure databases

ProteinModelPortalQ5XIH4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000003779.

Proteomic databases

PaxDbQ5XIH4.
PRIDEQ5XIH4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000003779; ENSRNOP00000003779; ENSRNOG00000002759.
GeneID305348.
KEGGrno:305348.

Organism-specific databases

CTD11019.
RGD1307270. Lias.

Phylogenomic databases

eggNOGCOG0320.
GeneTreeENSGT00390000006234.
HOGENOMHOG000235998.
HOVERGENHBG023328.
InParanoidQ5XIH4.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG7P2XS7.
PhylomeDBQ5XIH4.
TreeFamTF300817.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Gene expression databases

GenevestigatorQ5XIH4.

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...

Other

NextBio654409.
PROQ5XIH4.

Entry information

Entry nameLIAS_RAT
AccessionPrimary (citable) accession number: Q5XIH4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: November 23, 2004
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways