C71AJ_PASSA
ID C71AJ_PASSA Reviewed; 473 AA.
AC C0SJS2;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Psoralen synthase {ECO:0000303|PubMed:19098286};
DE EC=1.14.14.141 {ECO:0000269|PubMed:19098286};
DE AltName: Full=Cytochrome P450 CYP71AJ3 {ECO:0000303|PubMed:19098286};
DE Flags: Fragment;
GN Name=CYP71AJ3 {ECO:0000303|PubMed:19098286};
OS Pastinaca sativa (Wild parsnip) (Anethum pastinaca).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Tordylieae; Tordyliinae; Pastinaca.
OX NCBI_TaxID=4041;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Demi-long de Guernesey;
RX PubMed=19098286; DOI=10.1074/jbc.m807351200;
RA Larbat R., Hehn A., Hans J., Schneider S., Jugde H., Schneider B.,
RA Matern U., Bourgaud F.;
RT "Isolation and functional characterization of CYP71AJ4 encoding for the
RT first P450 monooxygenase of angular furanocoumarin biosynthesis.";
RL J. Biol. Chem. 284:4776-4785(2009).
RN [2]
RP FUNCTION, REVIEW, PATHWAY, AND INDUCTION BY WOUNDING.
RC STRAIN=cv. Demi-long de Guernesey;
RX PubMed=29971079; DOI=10.3389/fpls.2018.00820;
RA Krieger C., Roselli S., Kellner-Thielmann S., Galati G., Schneider B.,
RA Grosjean J., Olry A., Ritchie D., Matern U., Bourgaud F., Hehn A.;
RT "The CYP71AZ P450 subfamily: A driving factor for the diversification of
RT coumarin biosynthesis in apiaceous plants.";
RL Front. Plant Sci. 9:820-820(2018).
CC -!- FUNCTION: Involved in the biosynthesis of coumarins and furanocoumarins
CC (FCs), natural products required for defense responses against attacks
CC by predators with potential medical and agroindustrial usages such as
CC anticoagulant, rodenticide and artificial vanilla substitutes
CC (PubMed:29971079). Involved in linear furanocumarin (psoralen)
CC biosynthesis (PubMed:19098286). Converts marmesin to psoralen and, with
CC much lower affinity, 5-hydroxymarmesin to bergaptol (PubMed:19098286).
CC {ECO:0000269|PubMed:19098286, ECO:0000303|PubMed:29971079}.
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:0000269|PubMed:19098286};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 uM for marmesin {ECO:0000269|PubMed:19098286};
CC KM=19 uM for 5-hydroxymarmesin {ECO:0000269|PubMed:19098286};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:19098286};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:29971079}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q6QNI4}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Accumulates in roots after wounding.
CC {ECO:0000269|PubMed:29971079}.
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. {ECO:0000305|PubMed:19098286}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; EF191020; ABO84853.1; -; mRNA.
DR AlphaFoldDB; C0SJS2; -.
DR SMR; C0SJS2; -.
DR BRENDA; 1.14.14.141; 4562.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
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:0102876; F:psoralen synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009805; P:coumarin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP: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..>473
FT /note="Psoralen synthase"
FT /id="PRO_0000401481"
FT TRANSMEM 1..17
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 350..355
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT BINDING 425
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:Q94IP1"
FT SITE 109
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT SITE 286
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT SITE 290
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT NON_TER 1
FT NON_TER 473
SQ SEQUENCE 473 AA; 53246 MW; 5E760F7E86215486 CRC64;
YFFPLFLVTI FLYKWLVKKT PSKNLPPSPP RLPIIGNLHQ IGPDPQISLR DLAREYGPVM
HLKFGSVPVL VVSSADGARE IFKTHDLVFA DRPYSSVANR IFYNGRDMVF ARYTEYWRQV
KSTCVTQLLS VKRVQSFHNV REEEVALLLD NIENSKSKVI NLSEMLIELT GNVVCRAALG
SGYNVDSYKS LLLQIMDMLG YSRSIEDFFP SLGWVDWITG LKGKVEKAAN GVDAFLEGVL
KNHTNPSTSS ANKDFVSILL EIQEADAGSS MDKECIKSLI WDMLGAGTET IATALEWTIG
ALIKSPDAMS KLQKEVREIG KGKSRIEEGD LVKMDYLKAV MKESMRLYFT APLLVPREAR
QDVKFMGYDI KSGTQVLINA WAIARDPSSW DNPEEFRPER FLNSPIDYKG FNYEYIPFGA
GRRGCPGIQF AISVNELVVA NVVNKFNFEL PDGKRLEEMD MTASTGITFH KKS
