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ANGS_PASSA
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   03-AUG-2022, entry version 47.
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:MON-15618; -.
DR   BRENDA; 1.14.14.148; 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: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   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..>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
 
 
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