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Protein

Lipoyl synthase 1, mitochondrial

Gene

PHATRDRAFT_18029

Organism
Phaeodactylum tricornutum (strain CCAP 1055/1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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. no protein annotated in this organism
  2. Lipoyl synthase 1, mitochondrial (PHATRDRAFT_18029), Lipoyl synthase 2, mitochondrial (PHATRDRAFT_28652)
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 bindingi117Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi122Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi128Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi148Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi152Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi155Iron-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 1, mitochondrial (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthase 1UniRule annotation
Short name:
LS 1UniRule annotation
Short name:
Lip-syn 1UniRule annotation
Lipoic acid synthase 1UniRule annotation
Gene namesi
ORF Names:PHATRDRAFT_18029
OrganismiPhaeodactylum tricornutum (strain CCAP 1055/1)
Taxonomic identifieri556484 [NCBI]
Taxonomic lineageiEukaryotaStramenopilesBacillariophytaBacillariophyceaeBacillariophycidaeNaviculalesPhaeodactylaceaePhaeodactylum
Proteomesi
  • UP000000759 Componentsi: Chromosome 2, Unassembled WGS sequence

Subcellular locationi

B7FRU7:
  • Mitochondrion UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 25MitochondrionUniRule annotationAdd BLAST25
ChainiPRO_000039824326 – 401Lipoyl synthase 1, mitochondrialAdd BLAST376

Proteomic databases

PRIDEiB7FRU7.

Interactioni

Protein-protein interaction databases

STRINGi2850.Phatr18029.

Structurei

3D structure databases

ProteinModelPortaliB7FRU7.
SMRiB7FRU7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000235998.
InParanoidiB7FRU7.
KOiK03644.
OMAiPYCDIDF.

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.

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

B7FRU7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWSSSSSLCR NPSFRRAWLS TVTVTQTAAP TSSRLAALRT QLATEEASID
60 70 80 90 100
DFSSTNAPTT TTHYTSSNGS PIVRQKAAPR SAKILPKPRW LKAAPATSDN
110 120 130 140 150
YRKLRDTVRE LGLATVCEEA RCPNIGECWG GGEDQTATAT IMIMGDTCTR
160 170 180 190 200
GCRFCSVKTS RAPPPLDPHE PEKVATAIAQ WGLDYVVLTS VDRDDLPDQG
210 220 230 240 250
ADHFRQVVTQ LKLKKPSLLV EALTPDFQGN MDLVHAVATS GLDVYAHNME
260 270 280 290 300
TVEALTPKVR DRRATYRQSL EVLRYVKTIQ SDPIGTTNNH NNNNGCLTKT
310 320 330 340 350
SLMLGLGETD DQVLTTLRDL RDADVDVVTF GQYLQPTKKH LPVQEYVTPE
360 370 380 390 400
KFDFWQETAM GMGFAYVASG PLVRSSYKAG ELFLQKYIAQ KKQRNAEVAA

A
Length:401
Mass (Da):44,192
Last modified:February 10, 2009 - v1
Checksum:iC5270EA0E1E231A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000606 Genomic DNA. Translation: EEC50372.1.
RefSeqiXP_002177558.1. XM_002177522.1.
UniGeneiPtc.7635.

Genome annotation databases

EnsemblProtistsiPhatr3_J18029.t1; Phatr3_J18029.p1; Phatr3_J18029.
GeneIDi7197080.
KEGGipti:PHATRDRAFT_18029.

Similar proteinsi

Entry informationi

Entry nameiLIPA1_PHATC
AccessioniPrimary (citable) accession number: B7FRU7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 10, 2009
Last modified: October 25, 2017
This is version 47 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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