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Protein

Lipoyl synthase, mitochondrial

Gene

lias

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

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 N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(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

Pathwayi: 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)
  2. Lipoyl synthase, mitochondrial (lias), Lipoyl synthase, mitochondrial (lias), 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)DescriptionActionsGraphical viewLength
Metal bindingi113Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi118Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi144Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi148Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi151Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferaseUniRule annotation
Ligand4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionineUniRule annotation

Enzyme and pathway databases

ReactomeiR-XTR-389661. Glyoxylate metabolism and glycine degradation.
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:liasImported
Synonyms:LIASUniRule annotation
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)Imported
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
Proteomesi
  • UP000008143 Componenti: Unassembled WGS sequence

Organism-specific databases

XenbaseiXB-GENE-942448. lias.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

MitochondrionUniRule annotation

PTM / Processingi

Proteomic databases

PaxDbiF6WZH5.

Expressioni

Gene expression databases

BgeeiENSXETG00000012839.
ExpressionAtlasiF6WZH5. baseline.

Interactioni

Protein-protein interaction databases

STRINGi8364.ENSXETP00000028058.

Structurei

3D structure databases

ProteinModelPortaliF6WZH5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 340Elp3InterPro annotationAdd BLAST208

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
GeneTreeiENSGT00390000006234.
InParanoidiF6WZH5.
OMAiPYCDIDF.
OrthoDBiEOG091G0AXJ.
TreeFamiTF300817.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
PfamiView protein in Pfam
PF16881. LIAS_N. 1 hit.
PF04055. Radical_SAM. 1 hit.
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SFLDiSFLDS00029. Radical_SAM. 1 hit.
SMARTiView protein in SMART
SM00729. Elp3. 1 hit.
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

F6WZH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLCGLRRGA ELLRTCGLAE YHXKFLGGAK LPFQKFRIFF LTPKKGPPFP
60 70 80 90 100
FFSPFGFGTE IIVGPGLSAF NSGDCFSYYR LRLPPWVRTE IPMGKNYNKL
110 120 130 140 150
KNTLRNLNLH TVCEEARCPN NISDGGAEHI AKTVSLLKLM GDTCTRGCRF
160 170 180 190 200
CSVKTARNPP PLDPDEPFNT AKAIADWGLD YVVLTSVDRD DISDGGAEHI
210 220 230 240 250
AKTVSLLKER NQTILIECLT PDFRGNLKAV ETVAGSGLDV YAHNVETVPA
260 270 280 290 300
LQRHVRDPRA NFDQSVNVLK HAKNVRPELI SKTSIMLGLG ETDEQIYSTM
310 320 330 340 350
KALREAGVDC LTLGQYMQPT KRHLKVEEYI TPEKFKYWEK VGNELGFLYT
360 370
ASGPLVRSSY KAGEFFLKNL IERRKTKAV
Length:379
Mass (Da):42,481
Last modified:July 27, 2011 - v1
Checksum:iA9FC9CE2FCFA5CD3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAMC01023392 Genomic DNA. No translation available.
AAMC01023393 Genomic DNA. No translation available.
AAMC01023394 Genomic DNA. No translation available.
AAMC01023395 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENSXETT00000028058; ENSXETP00000028058; ENSXETG00000012839.

Similar proteinsi

Entry informationi

Entry nameiF6WZH5_XENTR
AccessioniPrimary (citable) accession number: F6WZH5
Entry historyiIntegrated into UniProtKB/TrEMBL: July 27, 2011
Last sequence update: July 27, 2011
Last modified: March 28, 2018
This is version 46 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteomeImported