PPSD_ASPOR
ID PPSD_ASPOR Reviewed; 528 AA.
AC Q2UAZ8;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cytochrome P450 monooxygenase ppsD {ECO:0000303|PubMed:32885554};
DE EC=1.-.-.- {ECO:0000305|PubMed:32885554};
DE AltName: Full=2,4'-dihydroxy-3'-methoxypropiophenone biosynthesis cluster protein D {ECO:0000303|PubMed:32885554};
GN Name=ppsD {ECO:0000303|PubMed:32885554}; ORFNames=AO090102000168;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32885554; DOI=10.1002/cbic.202000505;
RA Kan E., Tomita H., Katsuyama Y., Maruyama J.I., Koyama Y., Ohnishi Y.;
RT "Discovery of the 2,4'-dihydroxy-3'-methoxypropiophenone biosynthesis genes
RT in Aspergillus oryzae.";
RL ChemBioChem 22:203-211(2021).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of 2,4'-dihydroxy-3'-methoxypropiophenone
CC (PubMed:32885554). The first step of the pathway is the conversion of
CC acetate into acetyl-CoA by the acyl-CoA ligase ppsA (PubMed:32885554).
CC Acetyl-CoA is then used as a starter unit by the polyketide synthase
CC ppsB and condensed with 4 malonyl-CoA unit to produce the pentaketide
CC backbone (PubMed:32885554). During polyketide extension, the polykedite
CC chain is probably reduced and dehydrated by the KR and PT domains,
CC respectively (Probable). O-methylation seems to be catalyzed by an
CC unknown methyltransferase rather than by the CMeT domain of ppsB
CC (Probable). Two hydroxylations and one further decarboxylation step
CC catalyzed by yet unknown enzymes are then required to yield 4'-hydroxy-
CC 3'-methoxypropiophenone (Probable). PpsC functions as a carrier protein
CC to transport 4'-hydroxy-3'-methoxypropiophenone to a specific cell
CC compartment in which 4'-hydroxy-3'-methoxypropiophenone is hydroxylated
CC to 2,4'-dihydroxy-3'-methoxypropiophenone by a still to be identified
CC enzyme (PubMed:32885554). {ECO:0000269|PubMed:32885554,
CC ECO:0000305|PubMed:32885554}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Does not affecct the production of 2,4'-
CC dihydroxy-3'-methoxypropiophenone or 4'-hydroxy-3'-
CC methoxypropiophenone. {ECO:0000269|PubMed:32885554}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AP007162; BAE61267.1; -; Genomic_DNA.
DR RefSeq; XP_001822400.1; XM_001822348.1.
DR AlphaFoldDB; Q2UAZ8; -.
DR SMR; Q2UAZ8; -.
DR STRING; 510516.Q2UAZ8; -.
DR EnsemblFungi; BAE61267; BAE61267; AO090102000168.
DR GeneID; 5994445; -.
DR KEGG; aor:AO090102000168; -.
DR VEuPathDB; FungiDB:AO090102000168; -.
DR HOGENOM; CLU_001570_2_3_1; -.
DR OMA; SVPPVYQ; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..528
FT /note="Cytochrome P450 monooxygenase ppsD"
FT /id="PRO_0000451836"
FT TRANSMEM 2..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 441
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 528 AA; 59895 MW; 1732B23B620113D7 CRC64;
MLVLVSLVLC LTGFCLLQWA LKERKIVKGL PPGPRPKPII GNLLDLPPPG ALDWLHWLKH
KELYGPISSV TIFGQTIIII NGHRVANELM EKRSGVHSSR PHVPIAELAG WQYTLGFIPY
DSRLRAYRRA LHQEMGNATS ISKYHNILDM ETHRLLFRIL KTPDCLMQHL RKEAGSIILR
ITYGYITEPE AYDPLIDLVD KAMEDFAQVI LPGGWLVNFI PMLKYLPSWF PGCDWQRRAK
AFKQRAKAMT DIPYAFVKQQ HEQQKHIPSY VSRLLEQNNI KLGSEEELVV KWSAQSIYGG
GAETSVSVFA CFFQVMALHL NVQKKAQEEI DRVVGASRLP DLSDCKNLPY INAVVKEVLR
WHPVAPMGVA HASSKEDIYH RYVIPKGAIL VPNIWAMAHD PDFYHNAMDF EPERFLKSGR
NEQNPEYDPH QFIFGFGRRT CPGQHLVSAN LSLGVARVLA VFNITNAVRD GKKVPISPEF
SPGVISRPAP FELSIQVRNA ECKRLIEAVG MKFPWEESHA EALAQLRI
