ID   ABPB_ASPTN              Reviewed;         379 AA.
AC   Q0CX54;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Trans-prenyltransferase abpB {ECO:0000303|PubMed:28791090};
DE            EC=2.5.1.- {ECO:0000305|PubMed:28791090};
DE            EC=2.5.1.35 {ECO:0000305|PubMed:28791090};
DE   AltName: Full=Aspulvinone/butyrolactone prenyltransferase {ECO:0000303|PubMed:28791090};
GN   Name=abpB {ECO:0000303|PubMed:28791090}; ORFNames=ATEG_01730;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=28791090; DOI=10.1039/c5sc01058f;
RA   Guo C.J., Sun W.W., Bruno K.S., Oakley B.R., Keller N.P., Wang C.C.C.;
RT   "Spatial regulation of a common precursor from two distinct genes generates
RT   metabolite diversity.";
RL   Chem. Sci. 6:5913-5921(2015).
CC   -!- FUNCTION: Trans-prenyltransferase that acts in both the aspulvinones
CC       and butyrolactones pathways (PubMed:28791090). Prenylates aspulvinone E
CC       and butyrolactone II to yield repectively aspulvinone H and
CC       butyrolactone I (PubMed:28791090). {ECO:0000269|PubMed:28791090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aspulvinone E + 2 dimethylallyl diphosphate = aspulvinone H +
CC         2 diphosphate; Xref=Rhea:RHEA:13809, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57623, ChEBI:CHEBI:58013, ChEBI:CHEBI:58240; EC=2.5.1.35;
CC         Evidence={ECO:0000305|PubMed:28791090};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13810;
CC         Evidence={ECO:0000305|PubMed:28791090};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:28791090}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the accumulation of aspulvinone E and
CC       butyrolactone II. {ECO:0000269|PubMed:28791090}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH476595; EAU38487.1; -; Genomic_DNA.
DR   RefSeq; XP_001209095.1; XM_001209095.1.
DR   EnsemblFungi; EAU38487; EAU38487; ATEG_01730.
DR   GeneID; 4315774; -.
DR   VEuPathDB; FungiDB:ATEG_01730; -.
DR   HOGENOM; CLU_037431_0_0_1; -.
DR   OMA; LFARNHI; -.
DR   OrthoDB; 1531660at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
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   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..379
FT                   /note="Trans-prenyltransferase abpB"
FT                   /id="PRO_0000455465"
FT   BINDING         90..91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         338
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ   SEQUENCE   379 AA;  42297 MW;  05E0457541EDF33C CRC64;
     MTKSIIASEP PSAESSGRLP WKILGQTTGF PNQDQELWWL NTAPLLNEFL AECQYDVHLQ
     YQYLTFFRHH VIPVLGPFFA PGTTPNFASR LSKHGHPLDF SVNFQESGAT VRMSLGAIGS
     FAGLQQDPLN QFRAREVLDK LAILYPTVDL QLFKHFESEF GINHADALKV AAKLPKLDRA
     TKMIAIDMLK NGSMTFKVYY MVRSKAAATG LPVHTVLFNA VQRLGSAFEP GLSLLKQFLS
     PLCDAGETDL GLLSFDCVPT ESSRIKLYAI KQVGSLDAIR NLWTLGGTMD DPTTMKGLAV
     LEHVCELLQF GWSGDSRVQP ILFNYEIKKG STPKPQIYIP LADRYDEFDA AKLKAVFQDL
     DWKRVPFYQD TGKDLASVL