ID   C71AJ_AMMMJ             Reviewed;         494 AA.
AC   Q6QNI4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Psoralen synthase;
DE            EC=1.14.14.141 {ECO:0000250|UniProtKB:C0SJS4};
DE   AltName: Full=Cytochrome P450 CYP71AJ1;
GN   Name=CYP71AJ1;
OS   Ammi majus (Bishop's weed).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Ammi.
OX   NCBI_TaxID=48026;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND MUTAGENESIS OF MET-120.
RX   PubMed=17068340; DOI=10.1074/jbc.m604762200;
RA   Larbat R., Kellner S., Specker S., Hehn A., Gontier E., Hans J.,
RA   Bourgaud F., Matern U.;
RT   "Molecular cloning and functional characterization of psoralen synthase,
RT   the first committed monooxygenase of furanocoumarin biosynthesis.";
RL   J. Biol. Chem. 282:542-554(2007).
CC   -!- FUNCTION: Involved in linear furanocumarin (psoralen) biosynthesis.
CC       Converts marmesin to psoralen. {ECO:0000269|PubMed:17068340}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7S)-marmesin + O2 + reduced [NADPH--hemoprotein reductase] =
CC         acetone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC         psoralen; Xref=Rhea:RHEA:19281, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:6695, ChEBI:CHEBI:15347, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:27616,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.141;
CC         Evidence={ECO:0000250|UniProtKB:C0SJS4};
CC   -!- ACTIVITY REGULATION: Inhibited by columbianetin.
CC       {ECO:0000269|PubMed:17068340}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.5 uM for marmesin {ECO:0000269|PubMed:17068340};
CC         KM=29.3 uM for 5-hydroxymarmesin {ECO:0000269|PubMed:17068340};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}. Microsome membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- INDUCTION: By fungal elicitor extracted from Phytophthora sojae cell
CC       wall. {ECO:0000269|PubMed:17068340}.
CC   -!- BIOTECHNOLOGY: Psoralen possesses photocarcinogen properties. It
CC       intercalates in double-stranded DNA and cross-links pyrimidine bases
CC       under UV-A irradiation. Psoralen is widely used in combination with UV-
CC       A radiation to treat a variety of skin disorders like psoriasis or
CC       eczema.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY532370; AAT06911.1; -; mRNA.
DR   AlphaFoldDB; Q6QNI4; -.
DR   SMR; Q6QNI4; -.
DR   KEGG; ag:AAT06911; -.
DR   BioCyc; MetaCyc:MON-12571; -.
DR   BRENDA; 1.14.14.141; 296.
DR   SABIO-RK; Q6QNI4; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR   GO; GO:0102876; F:psoralen synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..494
FT                   /note="Psoralen synthase"
FT                   /id="PRO_0000395199"
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         436
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"
FT   MUTAGEN         120
FT                   /note="M->V: No effect on the activity."
FT                   /evidence="ECO:0000269|PubMed:17068340"
SQ   SEQUENCE   494 AA;  55891 MW;  D427BEAEFE327BC0 CRC64;
     MKMLEQNPQY LYFFSLFLVT IFLYKWLTLK KTPLKNLPPS PPQYPIIGNL HQIGPDPQAS
     LRDLAQKYGP LMFLKFGTVP VLVVSSADAA REALKTHDLV FADRPYSSVA NKIFYNGKDM
     VFARYTEYWR QVKSICVTQL LSNKRVNSFH YVREEEVDLL VQNLENSHSK VANLTELLIE
     VTGNVVCRVS VGSGDKVDSY KILILEIMDM LGYSRSIEDF FPLLGWVDWL TGLRGKVAEA
     AKGVDTFLEG VLKEHLSTTG SKYNDFVSIL LEIQEADAGS SMDNECIKSL IWDMLGAGTE
     TISTALEWTL AALIKNPDAM FKLQNEVREI GKGKSKISEA DLVKMNYLQA VMKESMRLYF
     TAPLLVPREA RQDIKFMGYD ISSGTQVLIN AWAIARDPLL WDKPEEFRPE RFLNSPIDYK
     GFHYEFLPFG AGRRGCPGIQ FAMCINELVV ANLVHKFNFE LPDGKRLEDL DMTAASGITL
     RKKSPLLVVA RPHV