SIRJ_LEPMC
ID SIRJ_LEPMC Reviewed; 394 AA.
AC Q6Q886;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Dipeptidase sirJ {ECO:0000305};
DE EC=3.4.13.19 {ECO:0000255|PROSITE-ProRule:PRU10073};
DE AltName: Full=Sirodesmin biosynthesis protein J {ECO:0000303|PubMed:15387811};
GN Name=sirJ {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: Dipeptidase; 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 -!- CATALYTIC ACTIVITY:
CC Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10073};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10073};
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 metallo-dependent hydrolases superfamily.
CC Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}.
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DR EMBL; AY553235; AAS92542.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6Q886; -.
DR SMR; Q6Q886; -.
DR OMA; EEVQNSC; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01301; rDP_like; 1.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR008257; Pept_M19.
DR PANTHER; PTHR10443; PTHR10443; 1.
DR Pfam; PF01244; Peptidase_M19; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE 2: Evidence at transcript level;
KW Dipeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Virulence; Zinc.
FT CHAIN 1..394
FT /note="Dipeptidase sirJ"
FT /id="PRO_0000437703"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
SQ SEQUENCE 394 AA; 43535 MW; 341456F2C7FEFDDB CRC64;
MKSEPGNEFL ERAANLLSRV PLIDGHNDWA NIIRGYYSNK IHVRNFSREE SLVGHVDIKK
LRKGLVGGTF WSAYVDCPAQ DKINVFNDDS YLETIRETLQ QIDLILRLIK KYPDDLELAT
TSSGILSSFQ NGKIASLLGI EGLHQIGNSP SVLRMFYNLG VRYATLTHNH NNAYADSATA
KTPVHNGLSI KGRAIIQEMN RLGMIIDLSH TSEQTAEDVL RQTRAPIIFS HSSAFGVHPH
PRNVKDNILH MLKSNKGLIM ISFVPEFSSA DPGLSSLMDV VKHIIYVGEL IGYDHVGIGS
DFDGMARAVL GLSDTSTFPR LVAELIANQI PEGDVEKIVG GNLIRVMGDV EAVAHRQCED
DILELEEEVK PLWDDAFKAK IAAAYPEALA LNAL
