SIRD_LEPMC
ID SIRD_LEPMC Reviewed; 448 AA.
AC Q6Q874;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=4-O-dimethylallyl-L-tyrosine synthase {ECO:0000303|PubMed:19762440};
DE EC=2.5.1.122 {ECO:0000269|PubMed:19762440};
DE AltName: Full=Sirodesmin biosynthesis protein P {ECO:0000303|PubMed:15387811};
DE AltName: Full=Tyrosine O-prenyltransferase sirD {ECO:0000303|PubMed:19762440};
GN Name=sirD {ECO:0000303|PubMed:19762440};
OS Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=5022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX PubMed=15387811; DOI=10.1111/j.1365-2958.2004.04215.x;
RA Gardiner D.M., Cozijnsen A.J., Wilson L.M., Pedras M.S., Howlett B.J.;
RT "The sirodesmin biosynthetic gene cluster of the plant pathogenic fungus
RT Leptosphaeria maculans.";
RL Mol. Microbiol. 53:1307-1318(2004).
RN [2]
RP FUNCTION.
RX PubMed=18272357; DOI=10.1016/j.mycres.2007.08.017;
RA Fox E.M., Howlett B.J.;
RT "Biosynthetic gene clusters for epipolythiodioxopiperazines in filamentous
RT fungi.";
RL Mycol. Res. 112:162-169(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=19762440; DOI=10.1099/mic.0.033886-0;
RA Kremer A., Li S.M.;
RT "A tyrosine O-prenyltransferase catalyses the first pathway-specific step
RT in the biosynthesis of sirodesmin PL.";
RL Microbiology 156:278-286(2010).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21038099; DOI=10.1007/s00253-010-2956-x;
RA Zou H.X., Xie X., Zheng X.D., Li S.M.;
RT "The tyrosine O-prenyltransferase SirD catalyzes O-, N-, and C-
RT prenylations.";
RL Appl. Microbiol. Biotechnol. 89:1443-1451(2011).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24083562; DOI=10.1021/cb400691z;
RA Rudolf J.D., Poulter C.D.;
RT "Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on
RT tyrosine and tryptophan derivatives.";
RL ACS Chem. Biol. 8:2707-2714(2013).
RN [6]
RP FUNCTION.
RX PubMed=27390873; DOI=10.1371/journal.pone.0158945;
RA Dopstadt J., Neubauer L., Tudzynski P., Humpf H.U.;
RT "The epipolythiodiketopiperazine gene cluster in Claviceps purpurea:
RT dysfunctional cytochrome P450 enzyme prevents formation of the previously
RT unknown clapurines.";
RL PLoS ONE 11:E0158945-E0158945(2016).
CC -!- FUNCTION: 4-O-dimethylallyl-L-tyrosine synthase; part of the gene
CC cluster that mediates the biosynthesis of sirodesmin PL, an
CC epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged
CC cyclic dipeptide and that acts as a phytotoxin which is involved in the
CC blackleg didease of canola (PubMed:15387811, PubMed:18272357,
CC PubMed:19762440). SirD catalyzes the O-prenylation of L-tyrosine (L-
CC Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O-
CC dimethylallyl-L-Tyr, and therefore represents probably the first
CC pathway-specific enzyme in the biosynthesis of sirodesmin PL
CC (PubMed:19762440, PubMed:21038099, PubMed:24083562). SirD can also use
CC D-tyrosine, L-3,4-dihydroxyphenylalanine, 4-amino-l-phenylalanine and
CC tryptophan derivatives as substrates, albeit with a lower transferase
CC activity (PubMed:19762440, PubMed:21038099, PubMed:24083562). 4-O-
CC dimethylallyl-L-Tyr, then undergoes condensation with L-Ser in a
CC reaction catalyzed by the non-ribosomal peptide synthase sirP to form
CC the diketopiperazine (DKP) backbone (PubMed:18272357). Further
CC bishydroxylation of the DKP performed by the cytochrome P450
CC monooxygenase sirC leads to the production of the intermediate
CC phomamide (PubMed:27390873). This step is essential to form the
CC reactive thiol group required for toxicity of sirodesmin PL
CC (PubMed:27390873). The next steps of sirodesmin biosynthesis are not
CC well understood yet, but some predictions could be made from
CC intermediate compounds identification (PubMed:18272357). Phomamide is
CC converted into phomalizarine via oxidation, probably by sirT
CC (PubMed:18272357). Further oxidation, methylation (by sirM or sirN) and
CC reduction steps convert phomalizarine to deacetyl sirodesmin
CC (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates
CC deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357).
CC {ECO:0000269|PubMed:19762440, ECO:0000269|PubMed:21038099,
CC ECO:0000269|PubMed:24083562, ECO:0000269|PubMed:27390873,
CC ECO:0000305|PubMed:15387811, ECO:0000305|PubMed:18272357}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + L-tyrosine = 4-O-dimethylallyl-L-
CC tyrosine + diphosphate; Xref=Rhea:RHEA:41584, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57623, ChEBI:CHEBI:58315, ChEBI:CHEBI:78314;
CC EC=2.5.1.122; Evidence={ECO:0000269|PubMed:19762440,
CC ECO:0000269|PubMed:21038099, ECO:0000269|PubMed:24083562};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for L-Tyr (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:19762440};
CC KM=0.17 mM for DMAPP (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:19762440};
CC KM=0.23 mM for L-tryptophan (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:19762440};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:15387811}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19762440}.
CC -!- INDUCTION: Expression is co-regulated with the other genes from the
CC sirodesmin cluster and corresponds with sirodesmin production
CC (PubMed:15387811). {ECO:0000269|PubMed:15387811}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY553235; AAS92554.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6Q874; -.
DR SMR; Q6Q874; -.
DR PRIDE; Q6Q874; -.
DR KEGG; ag:AAS92554; -.
DR OMA; IRYSFEP; -.
DR BRENDA; 2.5.1.122; 2984.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR InterPro; IPR012148; DMATS-type_fun.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR PIRSF; PIRSF000509; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 1: Evidence at protein level;
KW Transferase; Virulence.
FT CHAIN 1..448
FT /note="4-O-dimethylallyl-L-tyrosine synthase"
FT /id="PRO_0000430679"
SQ SEQUENCE 448 AA; 50986 MW; 8975C32362040265 CRC64;
MQTARLFQGN LNLAAANIRD YEKKEQRNLG VWLSLNQWLR LYDEDTRFWW TTTAPMLGRM
MELIGYDQDA QQKHLLFYYI YVLPSLGRRP SPEGYPTGWN SFMTDDYSPL ELSWDWGVAE
GESSVRFSIE PIGKYAGTQA DPLNQKMVYQ LVDGLRPAFH HTLDLTLFDV FSEALTTSRE
KFGTRKLSLE GRSQYFVAFD LDVGHPRLKA YFMPGLKSIE SNTPVSELVV KAMDACELHF
GSLFMQAFRR LNSDLEAFSA TSYHRPEIEI VGIDCVSPVK SRAKIYIRHR GTSFDSVCRM
LSMGAKAPLD AASVASLREL WALVLGLPKD FPSDQELPSV PHRTSGVLYY FEIKPTSDAI
VPKVYIPVRH YASNDLSIAQ GLATYFERRG QTVAAENYVD ALSDIFSHRS LDSGLGLHTY
ISCTFKKTGL SVTSYFNPEI YHPNRYRQ
