PYNI_ASPNC
ID PYNI_ASPNC Reviewed; 280 AA.
AC A5ABG7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Thioesterase pynI {ECO:0000303|PubMed:26414728};
DE EC=3.1.-.- {ECO:0000269|PubMed:26414728};
DE AltName: Full=Pyranonigrin biosynthesis cluster protein I {ECO:0000303|PubMed:26414728};
GN Name=pynI {ECO:0000303|PubMed:26414728}; ORFNames=An11g00320;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION.
RX PubMed=24106156; DOI=10.1002/cbic.201300430;
RA Awakawa T., Yang X.L., Wakimoto T., Abe I.;
RT "Pyranonigrin E: a PKS-NRPS hybrid metabolite from Aspergillus niger
RT identified by genome mining.";
RL ChemBioChem 14:2095-2099(2013).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=26414728; DOI=10.1021/acs.orglett.5b02435;
RA Yamamoto T., Tsunematsu Y., Noguchi H., Hotta K., Watanabe K.;
RT "Elucidation of pyranonigrin biosynthetic pathway reveals a mode of
RT tetramic acid, fused gamma-pyrone, and exo-methylene formation.";
RL Org. Lett. 17:4992-4995(2015).
CC -!- FUNCTION: Thioesterase; part of the gene cluster that mediates the
CC biosynthesis of pyranonigrins, a family of antioxidative compounds
CC (PubMed:24106156). The first step of pyranonigrins biosynthesis is
CC performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-
CC CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-
CC 6,8-dienyl-ACP (PubMed:24106156). The enoyl reducrase (ER) domain of
CC pynA is likely to be functional during the first two rounds of
CC polyketide chain extension, to generate the saturated C-C bonds of the
CC alkyl side chain (Probable). PynA subsequently forms the amide bond
CC between the acyl chain and L-serine (PubMed:24106156, PubMed:26414728).
CC Although pynA has a terminal reductase domain, it appears to require
CC the thioesterase pynI for the release of the straight-chain
CC intermediate from pynA via the formation of a tetramic acid
CC pyranonigrin J (PubMed:26414728). The methyltransferase pynC then
CC coverts pyranonigrin J to pyranonigrin I via N-methylation
CC (PubMed:26414728). The FAD-dependent monooxygenase pynG catalyzes an
CC epoxidation-mediated cyclization to form the dihydro-gamma-pyrone
CC moiety, followed by pynD-catalyzed oxidation of the alcohol to the
CC ketone and enolization to yield the characteristic tetramic acid-fused
CC gamma-pyrone core of pyranonigrin H (PubMed:26414728). Pyranonigrin H
CC is substrate of pynH for dehydration-mediated exo-methylene formation
CC from the serine side chain to produce pyranonigrin E, before the
CC oxidase pynE reduces the exo-methylene of pyranonigrin E into a pendant
CC methyl to form pyranonigrin G (PubMed:26414728). The FAD-linked
CC oxidoreductase pynB performs the reverse reaction and converts
CC pyranonigrin G back to pyranonigrin E (PubMed:26414728).
CC {ECO:0000269|PubMed:24106156, ECO:0000269|PubMed:26414728,
CC ECO:0000305|PubMed:24106156}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26414728}.
CC -!- DISRUPTION PHENOTYPE: Aabolishes the production of all pyranonigrins.
CC {ECO:0000269|PubMed:26414728}.
CC -!- SIMILARITY: Belongs to the AMT4 thioesterase family. {ECO:0000305}.
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DR EMBL; AM270218; CAK48265.1; -; Genomic_DNA.
DR AlphaFoldDB; A5ABG7; -.
DR SMR; A5ABG7; -.
DR PaxDb; A5ABG7; -.
DR EnsemblFungi; CAK48265; CAK48265; An11g00320.
DR VEuPathDB; FungiDB:An11g00320; -.
DR HOGENOM; CLU_057355_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0019748; P:secondary metabolic process; IGC:AspGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001031; Thioesterase.
DR Pfam; PF00975; Thioesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..280
FT /note="Thioesterase pynI"
FT /id="PRO_0000450061"
FT REGION 136..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 280 AA; 31176 MW; 8D95DE9AF99C307E CRC64;
MEPILHIQGD AHSSLTPLIF IHAVSGLAWP YMALGNLSNT SDPARSRPVY GISSPVYSSE
LQPHGPYLLG GWSMGGMIAV KMAEILQAKK ETVQQVILLD SINPEKYPAF VNEEEHRIIA
DGLFTNVCQA MGMADLADDS DDEDNRSDAS DASDDGSTMS DEEEEDDNLH RLFSTMRRHI
HASTLSISST EPGKLLPPNS VCHTSVTLVK CTQLSETVPA LFSARQRCIR RCALHPTLQW
RPQNFDRFRT LLIDARHDSL FDEEHVEEVT SMLRQILESC
