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Protein

Isomerase trt14

Gene

trt14

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Isomerase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin (PubMed:22549923, PubMed:23116177, PubMed:25671343). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 (PubMed:22549923, PubMed:23116177). DMOA is then prenylated into farnesyl-DMOA by the polyprenyl transferase trt2 (PubMed:22549923, PubMed:22782788, PubMed:23116177). Methylation by the methyltransferase trt5 then leads to farnesyl-DMOA methyl ester which is further subject to epoxidation by the FAD-dependent monooxygenase trt8 to yield epoxyfarnesyl-DMOA methyl ester (PubMed:22549923, PubMed:22782788, PubMed:23116177). Cyclization of epoxyfarnesyl-DMOA methyl ester by the terpene cyclase trt1 leads to a tetracycle intermediate which is in turn converted to preterretonin (PubMed:22549923, PubMed:22782788, PubMed:23116177). Dehydrogenase trt9 comes next to transform preterretonin to preterrenoid (PubMed:22549923, PubMed:23116177). The FAD-dependent monooxygenase trt3 is then required for the C-hydroxylation at C16 of preterrenoid to yield terrenoid (PubMed:22549923, PubMed:23116177). The cytochrome P450 trt6 catalyzes three successive oxidations to transform terrenoid into an unstable intermediate, which then undergoes the D-ring expansion and unusual rearrangement of the methoxy group to afford the core skeleton of terretonin (PubMed:25671343). This unprecedented rearrangement is catalyzed by the isomerase trt14 (PubMed:25671343). Finally, the nonheme iron-dependent dioxygenase trt7 accomplishes the last two oxidation reactions steps to complete the biosynthesis of terretonin (PubMed:25671343). Terretonin C is produced via spontaneous decarboxylation of the terretonin precursor (PubMed:23116177). Another shunt product of the terretonin biosynthesis is dihydrofarnesyl-DMOA, derived from epoxyfarnesyl-DMOA through hydrolysis of the epoxide (PubMed:22549923, PubMed:22782788, PubMed:23116177).4 Publications

Pathwayi: terpenoid biosynthesis

This protein is involved in the pathway terpenoid biosynthesis, which is part of Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway terpenoid biosynthesis and in Secondary metabolite biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase

Enzyme and pathway databases

UniPathwayiUPA00213

Names & Taxonomyi

Protein namesi
Recommended name:
Isomerase trt141 Publication (EC:5.-.-.-1 Publication)
Alternative name(s):
Terretonin synthesis protein 141 Publication
Gene namesi
Name:trt141 Publication
ORF Names:ATEG_10082
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000007963 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ATEG_10082

Pathology & Biotechi

Disruption phenotypei

Impairs the synthesis of terretonin but accumulates terretonin C (PubMed:23116177).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004365991 – 142Isomerase trt14Add BLAST142

Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 21Combined sources17
Helixi24 – 27Combined sources4
Turni28 – 30Combined sources3
Beta strandi31 – 39Combined sources9
Helixi42 – 44Combined sources3
Beta strandi46 – 48Combined sources3
Helixi50 – 61Combined sources12
Beta strandi64 – 72Combined sources9
Helixi74 – 76Combined sources3
Beta strandi78 – 80Combined sources3
Turni81 – 84Combined sources4
Beta strandi85 – 96Combined sources12
Beta strandi99 – 111Combined sources13
Beta strandi115 – 125Combined sources11
Helixi127 – 138Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5WQFX-ray2.00A/B/C/D/E/F1-142[»]
5WQGX-ray2.30A/B/C/D/E/F1-142[»]
5WQHX-ray2.10A/B/C/D/E/F1-142[»]
5WQIX-ray1.90A/B/C/D/E/F1-142[»]
SMRiQ0C8A2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000201243
OMAiVGAYENE
OrthoDBiEOG092C5G4H

Sequencei

Sequence statusi: Complete.

Q0C8A2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPTREDLVA TAKLFIAKYN EFTPESIISV RTPNSVSHRL FPTRNATRNI
60 70 80 90 100
GESMEACANA KEVFKSLTVS VIDDNDTIVD ERTRKVVFYL ASRGDTIVGE
110 120 130 140
WKSECIFIFQ MSEDGKLVDR IWAGFDTAYM DEFESRLDGI TF
Length:142
Mass (Da):16,134
Last modified:October 17, 2006 - v1
Checksum:i7598D4A2D31C9D1A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476609 Genomic DNA Translation: EAU29531.1
RefSeqiXP_001209384.1, XM_001209384.1

Genome annotation databases

EnsemblFungiiCADATEAT00002384; CADATEAP00002384; CADATEAG00002384
GeneIDi4319489

Entry informationi

Entry nameiTRT14_ASPTN
AccessioniPrimary (citable) accession number: Q0C8A2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 6, 2016
Last sequence update: October 17, 2006
Last modified: November 22, 2017
This is version 32 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

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health