SIRO_LEPMC
ID SIRO_LEPMC Reviewed; 329 AA.
AC Q6Q875;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Oxidoreductase sirO {ECO:0000303|PubMed:15387811};
DE EC=1.1.1.- {ECO:0000305};
DE AltName: Full=Sirodesmin biosynthesis protein O {ECO:0000303|PubMed:15387811};
GN Name=sirO {ECO:0000303|PubMed:15387811};
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], AND FUNCTION.
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.
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.
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.
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: Oxidoreductase; part of the gene cluster that mediates the
CC biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP)
CC characterized by a disulfide bridged cyclic dipeptide and that acts as
CC a phytotoxin which is involved in the blackleg didease of canola
CC (PubMed:15387811, PubMed:18272357, PubMed:19762440). SirD catalyzes the
CC O-prenylation of L-tyrosine (L-Tyr) in the presence of dimethylallyl
CC diphosphate (DMAPP) to yield 4-O-dimethylallyl-L-Tyr, and therefore
CC represents probably the first pathway-specific enzyme in the
CC biosynthesis of sirodesmin PL (PubMed:19762440, PubMed:21038099,
CC PubMed:24083562). 4-O-dimethylallyl-L-Tyr, then undergoes condensation
CC with L-Ser in a reaction catalyzed by the non-ribosomal peptide
CC synthase sirP to form the diketopiperazine (DKP) backbone
CC (PubMed:18272357). Further bishydroxylation of the DKP performed by the
CC cytochrome P450 monooxygenase sirC leads to the production of the
CC intermediate phomamide (PubMed:27390873). This step is essential to
CC form the 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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:15387811}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
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DR EMBL; AY553235; AAS92553.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6Q875; -.
DR SMR; Q6Q875; -.
DR OMA; PMAGGFL; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Virulence.
FT CHAIN 1..329
FT /note="Oxidoreductase sirO"
FT /id="PRO_0000437718"
FT ACT_SITE 59
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 54
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 148..149
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 203..213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 288..296
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT SITE 82
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:O43488"
SQ SEQUENCE 329 AA; 35959 MW; 3EA7144F138FC184 CRC64;
MSPSAHPDAP IIIFGTANFG SPEDSKGKLF GPVTVEQGRE YLDVLQEFNV DVLDTARIYS
GGESEKLLGA LDASREFKMC TKASGTLDGC GTRDAVLSAF KASSEALGVK EVDTYYLHTP
DRTTSLEETM DTINELHKAG SFKTFGISNL RADEVQHLHT YARSKNYILP TIYQGTYNLL
SRQCETKLLP LLRTLGIRFY AYSPLCCGLL INAEAKLQAS TGRWDTSHFG GKFMNALYNK
PSYIAASNAF QDMCGKYGVR PAGAAYRWVR YHSELEGGLG DGMVVGASSA RQLEESLGEI
EKGPLEEGLV GELEGLWDLV KEDAPAYSL
