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Protein

Lipoyl synthase, mitochondrial

Gene

PTRG_06961

Organism
Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) (Drechslera tritici-repentis)
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

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 (PTRG_07192)
  2. Lipoyl synthase, mitochondrial (PTRG_06961)
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 bindingi132Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi137Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi143Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi163Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi167Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi170Iron-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:PTRG_06961
OrganismiPyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) (Drechslera tritici-repentis)
Taxonomic identifieri426418 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaePyrenophora
Proteomesi
  • UP000001471 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
Transit peptidei1 – 30MitochondrionUniRule annotationAdd BLAST30
ChainiPRO_000039828531 – 417Lipoyl synthase, mitochondrialAdd BLAST387

Proteomic databases

PRIDEiB2WBE8

Interactioni

Protein-protein interaction databases

STRINGi426418.XP_001937293.1

Structurei

3D structure databases

ProteinModelPortaliB2WBE8
SMRiB2WBE8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
InParanoidiB2WBE8
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
SFLDiSFLDF00271 lipoyl_synthase, 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.

B2WBE8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSIPRSRC FLTSSTLKVV PRSRTPLRSF ATTSDTPQTS VPEAPGKRSR
60 70 80 90 100
PPTSFSDTLN AGPSFGDFVN PNAPLSPTEA YEIKTVQVGP EGRKKTITRL
110 120 130 140 150
PEWLRTPIPS NANQNYKQIK KDLRGLNLAT VCEEARCPNI SDCWGGSSKS
160 170 180 190 200
AATATIMLMG DTCTRGCRFC AVKTSKAPPP LDPHEPENTA EALRRWGLGY
210 220 230 240 250
VVITVVDRDD LADSGAHHIA ETIMKIKQKN PTQLVELLGG DYGGNLEMAK
260 270 280 290 300
VVARSGVDVF AHNIETTERL TPFVRDRRAK FRQSLDVLRS AKEERPELIT
310 320 330 340 350
KTSMMLGLGE TDEDLWHALR ELRANNVDVV TFGQYMRPTK RHMAVHDYVT
360 370 380 390 400
PDKFELWRQR ALDMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRLGSSAG
410
KNDVAELSAA EEVGKAL
Length:417
Mass (Da):46,079
Last modified:July 1, 2008 - v1
Checksum:i56EB27FD34072E72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231621 Genomic DNA Translation: EDU49880.1
RefSeqiXP_001937293.1, XM_001937258.1

Genome annotation databases

EnsemblFungiiEDU49880; EDU49880; PTRG_06961
GeneIDi6345232

Similar proteinsi

Entry informationi

Entry nameiLIPA_PYRTR
AccessioniPrimary (citable) accession number: B2WBE8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 1, 2008
Last modified: July 18, 2018
This is version 54 of the entry and version 1 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

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