SIRQ_LEPMC
ID SIRQ_LEPMC Reviewed; 393 AA.
AC Q6Q888;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Short chain dehydrogenase sirQ {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Sirodesmin biosynthesis protein Q {ECO:0000303|PubMed:15387811};
GN Name=sirQ {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: Short chain dehydrogenase; part of the gene cluster that
CC 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). 4-O-dimethylallyl-
CC L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed
CC by the non-ribosomal peptide synthase sirP to form the diketopiperazine
CC (DKP) backbone (PubMed:18272357). Further bishydroxylation of the DKP
CC performed by the cytochrome P450 monooxygenase sirC leads to the
CC production of the intermediate phomamide (PubMed:27390873). This step
CC is essential to form the reactive thiol group required for toxicity of
CC sirodesmin PL (PubMed:27390873). The next steps of sirodesmin
CC biosynthesis are not well understood yet, but some predictions could be
CC made from intermediate compounds identification (PubMed:18272357).
CC Phomamide is converted into phomalizarine via oxidation, probably by
CC sirT (PubMed:18272357). Further oxidation, methylation (by sirM or
CC sirN) and 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 short-chain dehydrogenases/reductases (SDR)
CC family. Highly divergent. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether sirQ is an active short chain
CC dehydrogenase since it lacks the conserved active sites. {ECO:0000305}.
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DR EMBL; AY553235; AAS92540.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6Q888; -.
DR SMR; Q6Q888; -.
DR OMA; FQEHIEI; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Virulence.
FT CHAIN 1..393
FT /note="Short chain dehydrogenase sirQ"
FT /id="PRO_0000437717"
FT BINDING 10..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 38..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 61..62
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 130
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 196
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 204..206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
SQ SEQUENCE 393 AA; 43905 MW; 689426C0FC9D67C7 CRC64;
MAVAVVFGAS GISGWGITKA LLDAKTQNAF SKIIALTNRS LSLAESGLPD DDRLQLHSGI
DLQANVDDVI AKLRERIPSI GNVTHVFYTA FSTSHTDNQL MMKASNTKML RTMVEAMETV
APSLSFIAVQ TGSNHYGILF AEVLGERFGP VPLKEDLPRL PSPLRDSLMF YAMADEMDEL
SRGKSWKWCD IRPDMIVGYL PRPNSHSIAE SIGYYLAFHA YLTPGEEVPF PGSEAAWNAK
FSLTGQGVLG NFNVHLACKN SIENGEAFNI ANKPFTTWAS LWPLLAGYWG LKGTAPVGHH
GIPDAASWVL DNMDRVKGWE EKYSMKPGRL FKIPWRYFHW ALNMPFDRYL DLTRCEQTGF
QQHEEHKESF ETAWKCMQEA KLLPIVDKSS TPP
