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Protein

Lipoyl synthase, mitochondrial

Gene

lias

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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.UniRule annotation

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathway: protein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Putative lipoyltransferase 2, mitochondrial (lipt2), Putative lipoyltransferase 2, mitochondrial (lipt2)
  2. Lipoyl synthase, mitochondrial (lias)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi128 – 1281Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi133 – 1331Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi139 – 1391Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi159 – 1591Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi166 – 1661Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
Name:lias
ORF Names:zgc:66080
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componenti: Unplaced

Organism-specific databases

ZFINiZDB-GENE-040426-1528. lias.

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1414MitochondrionUniRule annotationAdd
BLAST
Chaini15 – 399385Lipoyl synthase, mitochondrialPRO_0000398211Add
BLAST

Expressioni

Gene expression databases

BgeeiQ6PHG4.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000035286.

Structurei

3D structure databases

ProteinModelPortaliQ6PHG4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
HOVERGENiHBG023328.
InParanoidiQ6PHG4.
KOiK03644.
OrthoDBiEOG7P2XS7.
PhylomeDBiQ6PHG4.
TreeFamiTF300817.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6PHG4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALISRSCGA ASRYSSSHLF LPSKGAEAAN VYCNRLSTAA STSSSSSPSP
60 70 80 90 100
STHNDRKKDL REDGLNLQDF ISGELSEKSK WEEYRGNLKR EKGERLRLPP
110 120 130 140 150
WLKTEIPIGK NYNKLKNTLR ELNLHTVCEE ARCPNIGECW GGGEYATATA
160 170 180 190 200
TIMLMGDTCT RGCRFCSVKT ARRPPPLDPD EPYNTAKAIA AWGLDYVVLT
210 220 230 240 250
SVDRDDIPDG GAEHFAKTVS NIKERNSKIL VECLTPDFRG DLAAVEKIAL
260 270 280 290 300
SGLDVYAHNV ETVRELQRHV RDPRANFDQS LSVLRHAKKV KSSVLTKTSI
310 320 330 340 350
MLGLGETDAQ IQATLTELRD SGVDCLTLGQ YMQPTKRHLK VEEYVTPEKF
360 370 380 390
AFWEKVGQEM GFIYTASGPL VRSSYKAGEF FLKNLLEKRK TEETTATAE
Length:399
Mass (Da):44,394
Last modified:July 5, 2004 - v1
Checksum:iEAC52976CBE8D63D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 512Missing in AAI54782 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC154781 mRNA. Translation: AAI54782.1.
BC056561 mRNA. Translation: AAH56561.1.
RefSeqiNP_001103871.1. NM_001110401.1.
UniGeneiDr.16722.

Genome annotation databases

GeneIDi393528.
KEGGidre:393528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC154781 mRNA. Translation: AAI54782.1.
BC056561 mRNA. Translation: AAH56561.1.
RefSeqiNP_001103871.1. NM_001110401.1.
UniGeneiDr.16722.

3D structure databases

ProteinModelPortaliQ6PHG4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000035286.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi393528.
KEGGidre:393528.

Organism-specific databases

CTDi11019.
ZFINiZDB-GENE-040426-1528. lias.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
HOVERGENiHBG023328.
InParanoidiQ6PHG4.
KOiK03644.
OrthoDBiEOG7P2XS7.
PhylomeDBiQ6PHG4.
TreeFamiTF300817.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Miscellaneous databases

NextBioi20814551.
PROiQ6PHG4.

Gene expression databases

BgeeiQ6PHG4.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiLIAS_DANRE
AccessioniPrimary (citable) accession number: Q6PHG4
Secondary accession number(s): A8WGN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 5, 2004
Last modified: May 27, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.