SIRI_LEPMC
ID SIRI_LEPMC Reviewed; 413 AA.
AC Q6Q887;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Probable aminotransferase sirI {ECO:0000250|UniProtKB:Q4WMJ9};
DE EC=2.6.1.- {ECO:0000250|UniProtKB:Q4WMJ9};
DE AltName: Full=Sirodesmin biosynthesis protein I {ECO:0000303|PubMed:15387811};
GN Name=sirI {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], 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.
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: Probable aminotransferase; 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P00509};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:15387811}.
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 class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY553235; AAS92541.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6Q887; -.
DR SMR; Q6Q887; -.
DR OMA; CDPEDGV; -.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase; Pyridoxal phosphate; Transferase; Virulence.
FT CHAIN 1..413
FT /note="Probable aminotransferase sirI"
FT /id="PRO_0000437720"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P00509"
SQ SEQUENCE 413 AA; 45763 MW; 825C61073CB5CBD8 CRC64;
MLSQRSQRNT SEIIPRLLRE YHQPQAGNID ILDLSQAENS VLRDETLDEI RSAIGKHLNG
SNLSYPTGVG GELAARKSLA MFFNDRFNPA RSVSPDHIVM TPGASEALET LIFHICDPGE
GVLIAAPYWS GLDLALETRS LARIVQVNIP LHEFFEMSSI QYYERALATS PIPIKAILMC
NPHNPLGQCY NADVLEGLLG FCQRNKLHYI SDEVYGMSVF SDSDKGVTPA FTSILSHATA
PGLTSWVHMV YSLSKDFGCS GLRLGAIVTQ GNTDLLLGSA LITNNKVSSL TSVIVPSLLE
PRTTQKLLNQ NLRSRLNLNY GKVQRFLENR GLEFVPAKAG LFVFACLGKT RTEKEQLLLI
ECMKRSGVKL VAGTSFHFEQ FCWFRIMFSL PKNIVDVALQ RIGDALDETE KLL
