ANAPT_NEOFI
ID ANAPT_NEOFI Reviewed; 437 AA.
AC A1DN10;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Indole diterpene prenyltransferase anaPT {ECO:0000303|PubMed:19001367};
DE EC=2.5.1.- {ECO:0000269|PubMed:19001367, ECO:0000269|PubMed:19421461, ECO:0000269|PubMed:24014429, ECO:0000269|PubMed:24239009, ECO:0000269|PubMed:26294262};
DE AltName: Full=Acetylaszonalenin synthesis protein anaPT {ECO:0000303|PubMed:19001367};
GN Name=anaPT {ECO:0000303|PubMed:19001367}; ORFNames=NFIA_055300;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=19001367; DOI=10.1074/jbc.m807606200;
RA Yin W.B., Grundmann A., Cheng J., Li S.M.;
RT "Acetylaszonalenin biosynthesis in Neosartorya fischeri. Identification of
RT the biosynthetic gene cluster by genomic mining and functional proof of the
RT genes by biochemical investigation.";
RL J. Biol. Chem. 284:100-109(2009).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19421461; DOI=10.1039/b902413a;
RA Yin W.B., Cheng J., Li S.M.;
RT "Stereospecific synthesis of aszonalenins by using two recombinant
RT prenyltransferases.";
RL Org. Biomol. Chem. 7:2202-2207(2009).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20165805; DOI=10.1039/b922440h;
RA Yin W.B., Xie X.L., Matuschek M., Li S.M.;
RT "Reconstruction of pyrrolo[2,3-b]indoles carrying an alpha-configured
RT reverse C3-dimethylallyl moiety by using recombinant enzymes.";
RL Org. Biomol. Chem. 8:1133-1141(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24014429; DOI=10.1002/cbic.201300372;
RA Pockrandt D., Li S.M.;
RT "Geranylation of cyclic dipeptides by the dimethylallyl transferase AnaPT
RT resulting in a shift of prenylation position on the indole ring.";
RL ChemBioChem 14:2023-2028(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26294262; DOI=10.1021/acs.jnatprod.5b00422;
RA Zhou K., Yu X., Xie X., Li S.M.;
RT "Complementary flavonoid prenylations by fungal indole
RT prenyltransferases.";
RL J. Nat. Prod. 78:2229-2235(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS), AND CATALYTIC ACTIVITY.
RX PubMed=24239009; DOI=10.1016/j.chembiol.2013.10.007;
RA Yu X., Zocher G., Xie X., Liebhold M., Schutz S., Stehle T., Li S.M.;
RT "Catalytic mechanism of stereospecific formation of cis-configured
RT prenylated pyrroloindoline diketopiperazines by indole
RT prenyltransferases.";
RL Chem. Biol. 20:1492-1501(2013).
CC -!- FUNCTION: Indole diterpene prenyltransferase; part of the gene cluster
CC that mediates the biosynthesis of the prenylated pyrroloindoline
CC diketopiperazine acetylaszonalenin (PubMed:19001367). The first step in
CC the pathway is the formation of (R)-benzodiazepinedione by condensation
CC of tryptophan and anthranilic acid catalyzed by the non-ribosomal
CC peptide synthetase anaPS (PubMed:19001367). The prenyltransferase anaPT
CC then converts (R)-benzodiazepinedione to aszonalenin in the presence of
CC dimethylallyl diphosphate (DMAPP) via C3-prenylation (PubMed:19001367,
CC PubMed:19421461, PubMed:20165805, PubMed:24014429, PubMed:26294262).
CC The last step in the biosynthesis of acetylaszonalenin via acetylation
CC of aszonalenin at position N1 catalyzed by anaAT (PubMed:19001367,
CC PubMed:20165805). {ECO:0000269|PubMed:19001367,
CC ECO:0000269|PubMed:19421461, ECO:0000269|PubMed:20165805,
CC ECO:0000269|PubMed:24014429, ECO:0000269|PubMed:26294262}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=232 uM for (R)-benzodiazepinedione {ECO:0000269|PubMed:19001367,
CC ECO:0000269|PubMed:26294262};
CC KM=156 uM for dimethylallyl diphosphate (DMAPP)
CC {ECO:0000269|PubMed:19001367};
CC KM=160 uM for geranyl diphosphate (GPP)
CC {ECO:0000269|PubMed:24014429};
CC KM=260 uM for naringenin {ECO:0000269|PubMed:26294262};
CC KM=480 uM for 7-hydroxyflavanone {ECO:0000269|PubMed:26294262};
CC KM=290 uM for eriodictyol {ECO:0000269|PubMed:26294262};
CC KM=180 uM for silibinin {ECO:0000269|PubMed:26294262};
CC KM=810 uM for phloretin {ECO:0000269|PubMed:26294262};
CC KM=110 uM for apigenin {ECO:0000269|PubMed:26294262};
CC KM=510 uM for genistein {ECO:0000269|PubMed:26294262};
CC KM=110 uM for biochanin A {ECO:0000269|PubMed:26294262};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:19001367}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; DS027698; EAW16181.1; -; Genomic_DNA.
DR RefSeq; XP_001258078.1; XM_001258077.1.
DR PDB; 4LD7; X-ray; 2.83 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-437.
DR PDBsum; 4LD7; -.
DR AlphaFoldDB; A1DN10; -.
DR SMR; A1DN10; -.
DR EnsemblFungi; EAW16181; EAW16181; NFIA_055300.
DR GeneID; 4584593; -.
DR KEGG; nfi:NFIA_055300; -.
DR VEuPathDB; FungiDB:NFIA_055300; -.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR HOGENOM; CLU_037431_0_0_1; -.
DR OMA; YIYPRIK; -.
DR OrthoDB; 1531660at2759; -.
DR BioCyc; MetaCyc:MON-18807; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR InterPro; IPR012148; DMATS-type_fun.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR PIRSF; PIRSF000509; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alkaloid metabolism; Reference proteome; Transferase.
FT CHAIN 1..437
FT /note="Indole diterpene prenyltransferase anaPT"
FT /id="PRO_0000438417"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..103
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 111
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 45..64
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4LD7"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 241..256
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:4LD7"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:4LD7"
FT TURN 298..302
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 306..321
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 365..379
FT /evidence="ECO:0007829|PDB:4LD7"
FT HELIX 382..394
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:4LD7"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 405..416
FT /evidence="ECO:0007829|PDB:4LD7"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 420..427
FT /evidence="ECO:0007829|PDB:4LD7"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:4LD7"
SQ SEQUENCE 437 AA; 48811 MW; 2D3443E151CDCA3C CRC64;
MSPLSMQTDS VQGTAENKSL ETNGTSNDQQ LPWKVLGKSL GLPTIEQEQY WLNTAPYFNN
LLIQCGYDVH QQYQYLAFYH RHVLPVLGPF IRSSAEANYI SGFSAEGYPM ELSVNYQASK
ATVRLGCEPV GEFAGTSQDP MNQFMTREVL GRLSRLDPTF DLRLFDYFDS QFSLTTSEAN
LAASKLIKQR RQSKVIAFDL KDGAIIPKAY FFLKGKSLAS GIPVQDVAFN AIESIAPKQI
ESPLRVLRTF VTKLFSKPTV TSDVFILAVD CIVPEKSRIK LYVADSQLSL ATLREFWTLG
GSVTDSATMK GLEIAEELWR ILQYDDAVCS HSNMDQLPLV VNYELSSGSA TPKPQLYLPL
HGRNDEAMAN ALTKFWDYLG WKGLAAQYKK DLYANNPCRN LAETTTVQRW VAFSYTESGG
AYLTVYFHAV GGMKGNL
