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Q6PHG4 (LIAS_DANRE) 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
ORF Names:zgc:66080
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length399 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 Potential HAMAP-Rule MF_03123.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1414Mitochondrion Potential
Chain15 – 399385Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398211

Sites

Metal binding1281Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1331Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1391Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1591Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Experimental info

Sequence conflict50 – 512Missing in AAI54782. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6PHG4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: EAC52976CBE8D63D

FASTA39944,394
        10         20         30         40         50         60 
MALISRSCGA ASRYSSSHLF LPSKGAEAAN VYCNRLSTAA STSSSSSPSP STHNDRKKDL 

        70         80         90        100        110        120 
REDGLNLQDF ISGELSEKSK WEEYRGNLKR EKGERLRLPP WLKTEIPIGK NYNKLKNTLR 

       130        140        150        160        170        180 
ELNLHTVCEE ARCPNIGECW GGGEYATATA TIMLMGDTCT RGCRFCSVKT ARRPPPLDPD 

       190        200        210        220        230        240 
EPYNTAKAIA AWGLDYVVLT SVDRDDIPDG GAEHFAKTVS NIKERNSKIL VECLTPDFRG 

       250        260        270        280        290        300 
DLAAVEKIAL SGLDVYAHNV ETVRELQRHV RDPRANFDQS LSVLRHAKKV KSSVLTKTSI 

       310        320        330        340        350        360 
MLGLGETDAQ IQATLTELRD SGVDCLTLGQ YMQPTKRHLK VEEYVTPEKF AFWEKVGQEM 

       370        380        390 
GFIYTASGPL VRSSYKAGEF FLKNLLEKRK TEETTATAE 

« Hide

References

[1]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo and Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC154781 mRNA. Translation: AAI54782.1.
BC056561 mRNA. Translation: AAH56561.1.
RefSeqNP_001103871.1. NM_001110401.1.
UniGeneDr.16722.

3D structure databases

ProteinModelPortalQ6PHG4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000035286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000036448; ENSDARP00000035286; ENSDARG00000022845.
GeneID393528.
KEGGdre:393528.

Organism-specific databases

CTD11019.
ZFINZDB-GENE-040426-1528. lias.

Phylogenomic databases

eggNOGCOG0320.
GeneTreeENSGT00390000006234.
HOGENOMHOG000235998.
HOVERGENHBG023328.
InParanoidQ6PHG4.
KOK03644.
OrthoDBEOG7P2XS7.
PhylomeDBQ6PHG4.
TreeFamTF300817.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Gene expression databases

BgeeQ6PHG4.

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

NextBio20814551.
PROQ6PHG4.

Entry information

Entry nameLIAS_DANRE
AccessionPrimary (citable) accession number: Q6PHG4
Secondary accession number(s): A8WGN4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 5, 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