ID   USTYA_ASPFN             Reviewed;         213 AA.
AC   B8NM67;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Oxidase ustYa {ECO:0000303|PubMed:24841822};
DE            EC=1.-.-.- {ECO:0000305|PubMed:26703898};
DE   AltName: Full=Ustiloxin B biosynthesis protein Ya {ECO:0000303|PubMed:24841822};
GN   Name=ustYa {ECO:0000303|PubMed:24841822}; ORFNames=AFLA_094990;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24841822; DOI=10.1016/j.fgb.2014.04.011;
RA   Umemura M., Nagano N., Koike H., Kawano J., Ishii T., Miyamura Y.,
RA   Kikuchi M., Tamano K., Yu J., Shin-ya K., Machida M.;
RT   "Characterization of the biosynthetic gene cluster for the ribosomally
RT   synthesized cyclic peptide ustiloxin B in Aspergillus flavus.";
RL   Fungal Genet. Biol. 68:23-30(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=27166860; DOI=10.1002/anie.201602611;
RA   Ye Y., Minami A., Igarashi Y., Izumikawa M., Umemura M., Nagano N.,
RA   Machida M., Kawahara T., Shin-Ya K., Gomi K., Oikawa H.;
RT   "Unveiling the biosynthetic pathway of the ribosomally synthesized and
RT   post-translationally modified peptide ustiloxin B in filamentous fungi.";
RL   Angew. Chem. Int. Ed. 55:8072-8075(2016).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX   PubMed=26703898; DOI=10.1016/j.fgb.2015.12.010;
RA   Nagano N., Umemura M., Izumikawa M., Kawano J., Ishii T., Kikuchi M.,
RA   Tomii K., Kumagai T., Yoshimi A., Machida M., Abe K., Shin-ya K., Asai K.;
RT   "Class of cyclic ribosomal peptide synthetic genes in filamentous fungi.";
RL   Fungal Genet. Biol. 86:58-70(2016).
CC   -!- FUNCTION: Oxidase; part of the gene cluster that mediates the
CC       biosynthesis of the secondary metabolite ustiloxin B, an antimitotic
CC       tetrapeptide (PubMed:24841822, PubMed:27166860, PubMed:26703898).
CC       First, ustA is processed by the subtilisin-like endoprotease Kex2 that
CC       is outside the ustiloxin B gene cluster, at the C-terminal side of Arg-
CC       Lys, after transfer to Golgi apparatus through the endoplasmic
CC       reticulum (ER) (PubMed:24841822). Cleavage by KEX2 generates 16
CC       peptides YAIG-I to YAIG-XVI (PubMed:24841822). To process the precursor
CC       peptide further, at least two peptidases are necessary to cleave the N-
CC       terminal and C-terminal sides of the Tyr-Ala-Ile-Gly core peptide which
CC       serves as backbone for the synthesis of ustiloxin B, through
CC       cyclization and modification of the tyrosine with a non-protein coding
CC       amino acid, norvaline (PubMed:24841822). One of the two peptidases must
CC       be the serine peptidase ustP; and the other pepdidase is probably ustH
CC       (PubMed:24841822). Macrocyclization of the core peptide derived from
CC       ustA requires the tyrosinase ustQ, as well as the homologous oxidases
CC       ustYa and ustYb, and leads to the production of the first cyclization
CC       product N-desmethylustiloxin F (PubMed:27166860, PubMed:26703898). For
CC       the formation of N-desmethylustiloxin F, three oxidation steps are
CC       required, hydroxylation at the benzylic position, hydroxylation at
CC       either the aromatic ring of Tyr or beta-position of Ile, and oxidative
CC       cyclization (PubMed:27166860). UstQ may catalyze the oxidation of a
CC       phenol moiety, whereas the ustYa and ustYb are most likely responsible
CC       for the remaining two-step oxidations (PubMed:27166860). N-
CC       desmethylustiloxin F is then methylated by ustM to yield ustiloxin F
CC       which in turn substrate of the cytochrome P450 monooxygenase ustC which
CC       catalyzes the formation of S-deoxyustiloxin H (PubMed:27166860). The
CC       flavoprotein monooxygenases ustF1 and ustF2 then participate in the
CC       modification of the side chain of S-deoxyustiloxin H, leading to the
CC       synthesis of an oxime intermediate, via ustiloxin H (PubMed:27166860).
CC       Finally, carboxylative dehydration performed by the cysteine
CC       desulfurase-like protein ustD yields ustiloxin B (PubMed:27166860).
CC       {ECO:0000269|PubMed:24841822, ECO:0000269|PubMed:26703898,
CC       ECO:0000269|PubMed:27166860}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:26703898}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Decreases the production of ustiloxin B
CC       (PubMed:24841822, PubMed:26703898). {ECO:0000269|PubMed:24841822,
CC       ECO:0000269|PubMed:26703898}.
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DR   EMBL; EQ963480; EED49418.1; -; Genomic_DNA.
DR   RefSeq; XP_002381319.1; XM_002381278.1.
DR   AlphaFoldDB; B8NM67; -.
DR   SMR; B8NM67; -.
DR   STRING; 332952.B8NM67; -.
DR   EnsemblFungi; EED49418; EED49418; AFLA_094990.
DR   VEuPathDB; FungiDB:AFLA_094990; -.
DR   eggNOG; ENOG502S1UR; Eukaryota.
DR   HOGENOM; CLU_042941_4_2_1; -.
DR   OMA; FTIRHRN; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:InterPro.
DR   InterPro; IPR021765; UstYa-like.
DR   PANTHER; PTHR33365; PTHR33365; 1.
DR   Pfam; PF11807; UstYa; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..213
FT                   /note="Oxidase ustYa"
FT                   /id="PRO_0000437293"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   213 AA;  24399 MW;  B298922E77D6F1C4 CRC64;
     MAERSSNGYK EVPVRQSEES TIAEEEKDTL LEARSYSRRD RKRSRSKAVW FLIALLLLSN
     IGLLGGLIHY FRKTHHKEKD VPWLPPKTVG RGFVNINNDT ALPDQPGLDQ SLPHQRAMIS
     VFHQLHCIYM TREGYYAARE GNLDQVNAAH LMHCWDYLRQ AIMCHADTTL EWIPAPPNDK
     GSTGWGVEHT CGDFDAIARW AEDNRLKTTY GIH