Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase, mitochondrial

Gene

lias

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -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

Miscellaneous

This protein may be expected to contain an N-terminal transit peptide but none has been predicted.UniRule annotation

Catalytic activityi

Protein N6-(octanoyl)lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = protein N6-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [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 bindingi106Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi111Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi117Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi137Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi141Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi144Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionTransferase
Ligand4Fe-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
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6251515 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

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003982121 – 372Lipoyl synthase, mitochondrialAdd BLAST372

Proteomic databases

PRIDEiQ6GQ48

Structurei

3D structure databases

ProteinModelPortaliQ6GQ48
SMRiQ6GQ48
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG023328
KOiK03644

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
SFLDiSFLDG01058 lipoyl_synthase_like, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00510 lipA, 1 hit

Sequencei

Sequence statusi: Complete.

Q6GQ48-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQCGLVRAA QLLRTCGLAE WHTPYRALSS LPDEKKELIK NGPDLQDFLS
60 70 80 90 100
GELVDKSSWA AYKGDLKRQK GERLRLPPWV KTEIPMGKNY NKLKNTLRNL
110 120 130 140 150
NLHTVCEEAR CPNIGECWGG GEYGTATATI MLMGDTCTRG CRFCSVKTAR
160 170 180 190 200
NPPPLDPDEP YNTSKAIAEW GLDYVVLTSV DRDDISDGGA EHIAQTVSML
210 220 230 240 250
KERNKTILIE CLTPDFRGNM KAVETVAKSG LDVYAHNVET VPALQRHVRD
260 270 280 290 300
PRANFDQSLN VLKHAKNVRP DLVSKTSIML GLGETDEQIY STMKALREAG
310 320 330 340 350
VDCLTLGQYM QPTKRHLKVE EYITPEKFKY WEKAGNELGF LYTASGPLVR
360 370
SSYKAGEFFL KNLIEKRKTK AI
Length:372
Mass (Da):41,803
Last modified:July 19, 2004 - v1
Checksum:i905039EBFE3CC48C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC072900 mRNA Translation: AAH72900.1
RefSeqiNP_001085534.1, NM_001092065.1
UniGeneiXl.55041

Genome annotation databases

GeneIDi443960
KEGGixla:443960

Similar proteinsi

Entry informationi

Entry nameiLIAS_XENLA
AccessioniPrimary (citable) accession number: Q6GQ48
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 19, 2004
Last modified: May 23, 2018
This is version 72 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health