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

SNOG_00270

Organism
Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum)
Status
Reviewed-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

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. Octanoyltransferase (SNOG_00855)
  2. Lipoyl synthase, mitochondrial (SNOG_00270)
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 bindingi97Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi102Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi108Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi128Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi132Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi135Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

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
ORF Names:SNOG_00270
OrganismiPhaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum)
Taxonomic identifieri321614 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePhaeosphaeriaceaeParastagonospora
Proteomesi
  • UP000001055 Componenti: Unassembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole 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_00003982801 – 378Lipoyl synthase, mitochondrialAdd BLAST378

Proteomic databases

PRIDEiQ0V6U4

Interactioni

Protein-protein interaction databases

STRINGi13684.SNOT_00270

Structurei

3D structure databases

ProteinModelPortaliQ0V6U4
SMRiQ0V6U4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiQ0V6U4
KOiK03644
OrthoDBiEOG092C13O2

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.

Q0V6U4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTSIRHNYR LSAIITPTTA AQADTLNAGP SFGDFVAPDA PLSPAEAYEI
60 70 80 90 100
KTVQVGPEGR KKTITRLPEW LKTPIPSNAN YKKIKKDLRG LNLHTVCEEA
110 120 130 140 150
KCPNISDCWG GSDKSAATAT IMLGGDTCTR GCRFCSVKTS KAPPPLDPHE
160 170 180 190 200
PENTAEALSR WGLGYVVLTI VDRDDLADGG ARHAMETIMK IKQKAPSMLV
210 220 230 240 250
EALVGDYAGD AEMVKLVANS GLDVFAHNVE TTEALTPYVR DRRANFKQSL
260 270 280 290 300
NVLRIAKETK PELITKTSIM LGLGETEDEL WKALKDLRAN DVDVVTFGQY
310 320 330 340 350
MRPTKKHMAV HEYVTPDVFE MWRQRALDMG FLYCASGPLV RSSYKAGEAF
360 370
IENVIKKRRM GRGGQVGGAQ IAEMEKSA
Length:378
Mass (Da):41,504
Last modified:February 5, 2008 - v2
Checksum:i3254B8CED743ABF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH445325 Genomic DNA Translation: EAT91765.2
RefSeqiXP_001790961.1, XM_001790909.1

Genome annotation databases

EnsemblFungiiSNOT_00270; SNOT_00270; SNOG_00270
GeneIDi5967982
KEGGipno:SNOG_00270

Similar proteinsi

Entry informationi

Entry nameiLIPA_PHANO
AccessioniPrimary (citable) accession number: Q0V6U4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 5, 2008
Last modified: May 23, 2018
This is version 72 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health