ID ANGS_PASSA Reviewed; 478 AA.
AC C0SJS3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Angelicin synthase {ECO:0000303|PubMed:19098286};
DE EC=1.14.14.148 {ECO:0000269|PubMed:19098286};
DE AltName: Full=Cytochrome P450 CYP71AJ4 {ECO:0000303|PubMed:19098286};
DE Flags: Fragment;
GN Name=CYP71AJ4 {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,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
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, AND PATHWAY.
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 angular furanocumarin biosynthesis.
CC Converts (+)-columbianetin to angelicin (PubMed:19098286). Produces
CC also some hydroxycolumbianetin as a by-product (PubMed:19098286). No
CC activity with demethylsuberosin, (+)-marmesin, 5-hydroxymarmesin,
CC psoralen, bergaptol, xanthotoxol, bergapten, xanthotoxin,
CC isopimpinellin, cinnamic acid, 4-coumaric acid, 2-coumaric acid,
CC ferulic acid, coumarin, herniarin, scopoletin, or umbelliferone
CC (PubMed:19098286). The reaction mechanism is initiated by the
CC abstraction of syn-C-3'-hydrogen (PubMed:19098286).
CC {ECO:0000269|PubMed:19098286, ECO:0000303|PubMed:29971079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-columbianetin + O2 + reduced [NADPH--hemoprotein
CC reductase] = acetone + angelicin + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:27481, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15347, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28928,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:437678;
CC EC=1.14.14.148; Evidence={ECO:0000269|PubMed:19098286};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- ACTIVITY REGULATION: Not inhibited by (+)-marmesin, psoralen, 5- or 8-
CC methoxypsoralen and angelicin. {ECO:0000269|PubMed:19098286}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 uM for (+)-columbianetin {ECO:0000269|PubMed:19098286};
CC KM=1.4 uM for syn-[3'-D]columbianetin {ECO:0000269|PubMed:19098286};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:19098286};
CC Temperature dependence:
CC Optimum temperature is 27-30 degrees Celsius.
CC {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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; EF191021; ABO84854.1; -; mRNA.
DR AlphaFoldDB; C0SJS3; -.
DR SMR; C0SJS3; -.
DR KEGG; ag:ABO84854; -.
DR BioCyc; MetaCyc:MONOMER-15618; -.
DR BRENDA; 1.14.14.148; 4562.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0102995; F:angelicin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009805; P:coumarin biosynthetic process; IDA:UniProtKB.
DR CDD; cd11072; CYP71-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR47956:SF4; CYTOCHROME P450 71A16-RELATED; 1.
DR PANTHER; PTHR47956; CYTOCHROME P450 71B11-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 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..>478
FT /note="Angelicin synthase"
FT /id="PRO_0000401480"
FT TRANSMEM 1..17
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 357..361
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT BINDING 431
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 293
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT SITE 297
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT NON_TER 1
FT NON_TER 478
SQ SEQUENCE 478 AA; 54135 MW; 8ACB6CD76A0F6B04 CRC64;
YFFSLFLVTI FLYKWLAKKT PSKNLPPSPP RLPIIGNLHQ IGPDLHISLR DLARKYGPLM
QLQLGRIPVL VVSSAEATRE VLKTHDVVFS QRPITSAIDK LCYKGRDVAF SRYSEYWRQV
RSTCVTQLLS NSRVHSFHNI REEEVALLIQ NIENSASEVI NLGEQLIQLT RNVVCRVSVG
SEYLSGHKGK LYQKLLAEVT EMLAYTYSIG DFIPLLGWVD WLSGSKAKVE KTAKEVDAFL
EGALRDHIKT MASNKGSAND DFLSILLEIR EADAGSTLDE ECIKAIVWDM ILGGTETTST
TLEWIVAAII KNPDVMFKLQ KEVREIGKGK SKIEEVDLVK MNYLKAVMKE SMRLYITAFL
LPREAKQDVK LMGYDISSGT QVLINTWETA RDPSLWDNPE EFRPERFLNS PIDYKGLHYE
YLPFGGGRRG CPGIQFAMAV NELAVANVVY KFDFKMPDGE RFEDLDMSGV PGISLYRK
//
