OPAB_ASPUT
ID OPAB_ASPUT Reviewed; 575 AA.
AC A0A0C1E1L9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Cytochrome P450 monooxygenase opaB {ECO:0000303|PubMed:33004788};
DE EC=1.-.-.- {ECO:0000269|PubMed:33004788};
DE AltName: Full=Oxepinamide F biosynthesis cluster protein B {ECO:0000303|PubMed:33004788};
GN Name=opaB {ECO:0000303|PubMed:33004788}; ORFNames=HK57_00064;
OS Aspergillus ustus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=40382;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=3.3904;
RX PubMed=25706180; DOI=10.1371/journal.pone.0116089;
RA Pi B., Yu D., Dai F., Song X., Zhu C., Li H., Yu Y.;
RT "A genomics based discovery of secondary metabolite biosynthetic gene
RT clusters in Aspergillus ustus.";
RL PLoS ONE 10:e0116089-e0116089(2015).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=33004788; DOI=10.1038/s41467-020-18713-0;
RA Zheng L., Wang H., Fan A., Li S.M.;
RT "Oxepinamide F biosynthesis involves enzymatic D-aminoacyl epimerization,
RT 3H-oxepin formation, and hydroxylation induced double bond migration.";
RL Nat. Commun. 11:4914-4914(2020).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of oxepinamides, derivatives of anthranilyl-
CC containing tripeptides that share an oxepin ring and a fused
CC pyrimidinone moiety (PubMed:33004788). The nonribosomal peptide
CC synthetase (NRPS) opaA assembles the quinazolinone core with D-Phe
CC incorporation (PubMed:33004788). The first adenylation domain (A1) of
CC opaA loads and activates anthranilic acid whereas the second A domain
CC (A2) is for activating of L-Phe, which is then converted to D-form by
CC the E domain (PubMed:33004788). The third A domain (A3) is responsible
CC for L-Ile activation and the terminal condensation domain C3 for
CC cyclization and releasing the NRPS product protuboxepin K
CC (PubMed:33004788). The cytochrome P450 monooxygenase opaB then
CC catalyzes alone the oxepin ring formation to convert protuboxepin K
CC into protuboxepin A (PubMed:33004788). The flavoenzyme opaC installs
CC subsequently one hydroxyl group at the oxepin ring, accompanied by
CC double bond migration, to form 15-epi-oxepinamide E (PubMed:33004788).
CC The epimerase opaE changes the D-Phe residue back to L-form, leading to
CC oxepinamide E, which is further methylated at the hydroxyl group at C-
CC 12 by the O-methyltransferase OpaF to yield oxepinamide F
CC (PubMed:33004788). {ECO:0000269|PubMed:33004788}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:33004788}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of both oxepinamide F
CC and oxepinamide E and leads to the accumulation of protuboxepin K.
CC {ECO:0000269|PubMed:33004788}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; JOMC01000153; KIA75457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1E1L9; -.
DR EnsemblFungi; KIA75457; KIA75457; HK57_00064.
DR Proteomes; UP000053475; Unassembled WGS sequence.
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; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..575
FT /note="Cytochrome P450 monooxygenase opaB"
FT /id="PRO_0000452994"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 521
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 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 575 AA; 64288 MW; 3287BDE5FF1B590C CRC64;
MAVAPNVSDL QSGVVKASQM ARAALEHTLQ HHQLQDFILA AILASIILLI IRNSMLSPLR
GIPGPRLAGL TSLYEFYYDV IKNGTYAHQH PKMHQQYDST IIRISPNHVH IADPELFAIG
PAGSRFRKAR YYYNSIGMST AIGSHYDVEA HHRHRSTMAV GFSTKSLQAF DPIIVNYARE
IMDIIASRGL KGTPVVLSHH TQAYTIDVVA KISFGQPVGA MHEVGDHPPT VQAMDCFSNH
FNFTKHFPYW QLILPFMPTS AVKRIMPGVH YIKEVGTRLI TNLIEQRRIE GRLDEEYQEG
KGAIFETLLK PNPKKQYPAP DLNGLVEDAC AFLVGGSDTT GLTLQAVTLF VLRNPDVLCA
LRAELDSASE FIRDSFDIHQ VSKLPWLTAV IRETMRLLPP TPGPLPREVP PEGIRVGKYF
LPGGNANKGP GRQPGDAEFR PLSPAVCSLY ITIPASTQTQ KGSSRSVGWE KAVRAWWSGG
THSVVDHARV SDASTSCAYF VFSSSIICGR EQHTDERFLA CRVAWHELLA FLALLFLRFD
LELYESDETN LEWTEHMFTR IRAPVQVRIM KDRWA
