SIRH_LEPMC
ID SIRH_LEPMC Reviewed; 406 AA.
AC Q6Q889;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Acetyltransferase sirH {ECO:0000303|PubMed:18272357};
DE EC=2.3.1.- {ECO:0000305|PubMed:18272357};
DE AltName: Full=Sirodesmin biosynthesis protein H {ECO:0000303|PubMed:15387811};
GN Name=sirH {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: Acetyltransferase; 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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 wax synthase family. {ECO:0000305}.
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DR EMBL; AY553235; AAS92539.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6Q889; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR InterPro; IPR044851; Wax_synthase.
DR InterPro; IPR032805; Wax_synthase_dom.
DR PANTHER; PTHR31595; PTHR31595; 1.
DR Pfam; PF13813; MBOAT_2; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Membrane; Transferase; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..406
FT /note="Acetyltransferase sirH"
FT /id="PRO_0000437735"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 406 AA; 46127 MW; 0FCB370E7B8ED37A CRC64;
MVSAKLPSIF IEAQLPLIYA NIILAFALGP QAHTFRVCLT LPILLFLVCQ SLYREQNGPW
EDLLSNNSLV MFTVFVYIDW ILLQSPDREQ WHKLNNAKTE SNGPTKAKES GPPHGFFQRI
WFGCRIATAW RYIGWSCQVK NVPMEHSAGY PRRYFIARKS LRALAFYLMK ETLEVYTAST
PHGGWWDTQN TKPALSIKNV PLWHQFKYTW VHIFLAYATL EMANSILGVV SVILHLATPQ
ECPSAFGDLE DFFTVRKAWS TVWHQHMRRL TSTMGLFVAR DLMQLRKGSF QSKYVQLFVG
FGVSAGLHAG VALLCSKALN DDSALFFFGI QAPIIMLEDH VIAKGKSLGF KDSPLWRFIG
FVWTTLAIGF TCRAWVGSMI DNGMWVHARK KDSVIQGLLI NAIQQP
