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Q5BIP7 (LIAS_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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, 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length372 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 – 2727Mitochondrion Potential
Chain28 – 372345Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000332310

Sites

Metal binding1061Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1111Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1171Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5BIP7 [UniParc].

Last modified April 12, 2005. Version 1.
Checksum: AA6C54F92133B3A8

FASTA37242,035
        10         20         30         40         50         60 
MSLRCGGAVR TVGPRVFGRY VFSPVREVSF LPDEKKEFLQ SGPDLQEFIS GNLADKSTWD 

        70         80         90        100        110        120 
EYKGNLKRQK GERLRLPPWL KTEIPMGKNY NKLKNTLRNL NLHTVCEEAR CPNIGECWGG 

       130        140        150        160        170        180 
GEYATATATI MLMGDTCTRG CRFCSVKTAR NPPPLDANEP YNTAKAIAEW GLDYVVLTSV 

       190        200        210        220        230        240 
DRDDMPDGGA EHFAKTVSYL KERNPKILVE CLTPDFRGDL KAIEKVALSG LDVYAHNVET 

       250        260        270        280        290        300 
VPELQRKVRD PRANFDQSLR VLKHAKEVRP DVISKTSIML GLGENDEQVY ATMKALREAD 

       310        320        330        340        350        360 
VDCLTLGQYM QPTKRHLKVE EYITPEKFKY WEKVGNELGF HYTASGPLVR SSYKAGEFFL 

       370 
KNLVAKRKTK AL 

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT021177 mRNA. Translation: AAX31359.1.
RefSeqNP_001017944.1. NM_001017944.1.
UniGeneBt.9756.

3D structure databases

ProteinModelPortalQ5BIP7.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5BIP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000019299; ENSBTAP00000019299; ENSBTAG00000014520.
GeneID530865.
KEGGbta:530865.

Organism-specific databases

CTD11019.

Phylogenomic databases

eggNOGCOG0320.
GeneTreeENSGT00390000006234.
HOGENOMHOG000235998.
HOVERGENHBG023328.
InParanoidQ5BIP7.
KOK03644.
OMAEEYVTPE.
TreeFamTF300817.

Enzyme and pathway databases

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...

Other

NextBio20875341.

Entry information

Entry nameLIAS_BOVIN
AccessionPrimary (citable) accession number: Q5BIP7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 12, 2005
Last modified: April 16, 2014
This is version 60 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