ID   USTZ_USTVR              Reviewed;         140 AA.
AC   A0A063C1W0;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Dehydratase ustZ {ECO:0000303|PubMed:31050129};
DE            EC=1.-.-.- {ECO:0000305|PubMed:31050129};
DE   AltName: Full=Ustilaginoidins biosynthesis cluster protein Z {ECO:0000303|PubMed:31050129};
GN   Name=ustZ {ECO:0000303|PubMed:31050129}; ORFNames=UV8b_2087, UVI_02036170;
OS   Ustilaginoidea virens (Rice false smut fungus) (Villosiclava virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Ustilaginoidea.
OX   NCBI_TaxID=1159556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UV-8b;
RX   PubMed=24846013; DOI=10.1038/ncomms4849;
RA   Zhang Y., Zhang K., Fang A., Han Y., Yang J., Xue M., Bao J., Hu D.,
RA   Zhou B., Sun X., Li S., Wen M., Yao N., Ma L.J., Liu Y., Zhang M.,
RA   Huang F., Luo C., Zhou L., Li J., Chen Z., Miao J., Wang S., Lai J.,
RA   Xu J.R., Hsiang T., Peng Y.L., Sun W.;
RT   "Specific adaptation of Ustilaginoidea virens in occupying host florets
RT   revealed by comparative and functional genomics.";
RL   Nat. Commun. 5:3849-3849(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IPU010;
RX   PubMed=27151791; DOI=10.1128/genomea.00306-16;
RA   Kumagai T., Ishii T., Terai G., Umemura M., Machida M., Asai K.;
RT   "Genome sequence of Ustilaginoidea virens IPU010, a rice pathogenic fungus
RT   causing false smut.";
RL   Genome Announc. 4:0-0(2016).
RN   [3]
RP   FUNCTION, AND PATHWAY.
RC   STRAIN=IPU010;
RX   PubMed=31050129; DOI=10.1002/anie.201903759;
RA   Obermaier S., Thiele W., Fuertges L., Mueller M.;
RT   "Enantioselective phenol coupling by laccases in the biosynthesis of fungal
RT   dimeric naphthopyrones.";
RL   Angew. Chem. Int. Ed. 58:9125-9128(2019).
CC   -!- FUNCTION: Dehydratase; part of the gene cluster that mediates the
CC       biosynthesis of ustilaginoidins, dimeric gamma-naphthopyrones isolated
CC       from different fungal species (PubMed:31050129). The first step in the
CC       biosynthesis of ustilaginoidins is the production of gamma-
CC       naphthopyrone precursor YWA1 by the non-reducing polyketide synthase
CC       ustP, via condensation of one acetyl-CoA starter unit with 6 malonyl-
CC       CoA units (PubMed:31050129). YWA1 is then probably substrate of the
CC       ustZ to yield norrubrofusarin via a dehydration reaction (Probable). A
CC       key enzyme in the biosynthetic pathway is the laccase ustL, which
CC       catalyzes the oxidative dimerization of norrubrofusarin to
CC       ustilaginoidin A (PubMed:31050129). It can produce the M- and P-
CC       atropisomers in varying amounts, depending on the reaction conditions
CC       (PubMed:31050129). For the biosynthesis of 3-methylustilaginoid in
CC       derivatives such as chaetochromin A, a methylated derivative of YWA1 is
CC       required (Probable). The C-methylation is considered to be catalyzed by
CC       ustM, the phosphopantetheine attachment site of which indicates that it
CC       acts on the growing polyketide chain before release of the product
CC       (Probable). For the biosynthesis of chaetochromin A, it is assumed that
CC       saturation of the D2 double bond takes place before dimerization, and
CC       is probably catalyzed by an external reductase because no candidate
CC       gene was identified within the cluster (Probable).
CC       {ECO:0000269|PubMed:31050129, ECO:0000305|PubMed:31050129}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=YWA1 = H(+) + H2O + norrubrofusarin; Xref=Rhea:RHEA:62680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:133763,
CC         ChEBI:CHEBI:145839; Evidence={ECO:0000305|PubMed:31050129};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62681;
CC         Evidence={ECO:0000305|PubMed:31050129};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:31050129}.
CC   -!- SIMILARITY: Belongs to the tpcK family. {ECO:0000305}.
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DR   EMBL; BBTG02000019; GAO19111.1; -; Genomic_DNA.
DR   EMBL; JHTR01000008; KDB16995.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A063C1W0; -.
DR   SMR; A0A063C1W0; -.
DR   EnsemblFungi; KDB16995; KDB16995; UV8b_2087.
DR   HOGENOM; CLU_115019_0_0_1; -.
DR   OrthoDB; 1621831at2759; -.
DR   Proteomes; UP000054053; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR009799; EthD_dom.
DR   Pfam; PF07110; EthD; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
PE   3: Inferred from homology;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN           1..140
FT                   /note="Dehydratase ustZ"
FT                   /id="PRO_0000448923"
FT   DOMAIN          18..113
FT                   /note="EthD"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   140 AA;  15848 MW;  E4E7F10F1BF6D921 CRC64;
     MASHHQLLCL NILGFRKPGI STEDYRNYMV NVHAPLVAGL MEKYGFLHFT MSHASEQSPQ
     LMDQLYDAQF ANTASYDCCV QIVFPSIECF VNMKADPYFK QTVGPDHEKF ADTKRSQMMI
     GWFSPLLING QQTDSLSAAE