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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: 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 N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi132 – 1321Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi137 – 1371Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi143 – 1431Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi167 – 1671Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi170 – 1701Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-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
ProteomesiUP000001471: Unassembled WGS sequence

Subcellular locationi

Mitochondrion UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionUniRule annotationAdd
BLAST
Chaini31 – 417387Lipoyl synthase, mitochondrialPRO_0000398285Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB2WBE8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiB2WBE8.
OrthoDBiEOG79KPR7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliB2WBE8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDU49880; EDU49880; PTRG_06961.
GeneIDi6345232.

Phylogenomic databases

InParanoidiB2WBE8.
OrthoDBiEOG79KPR7.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-repentis, reveals transduplication and the impact of repeat elements on pathogenicity and population divergence."
    Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B., Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H., Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W., Schwartz D.C., Spatafora J.W.
    , Turgeon B.G., Yandava C., Young S., Zhou S., Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.
    G3 (Bethesda) 3:41-63(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pt-1C-BFP.

Entry informationi

Entry nameiLIPA_PYRTR
AccessioniPrimary (citable) accession number: B2WBE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 1, 2008
Last modified: January 7, 2015
This is version 39 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.