C71Z6_PASSA
ID C71Z6_PASSA Reviewed; 506 AA.
AC A0A2Z5D852;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=5-OH-xanthotoxin synthase {ECO:0000303|PubMed:29971079};
DE EC=1.14.14.- {ECO:0000269|PubMed:29971079};
DE AltName: Full=Cytochrome P450 CYP71AZ6 {ECO:0000303|PubMed:29971079};
GN Name=CYP71AZ6 {ECO:0000303|PubMed:29971079};
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, 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). Catalyzes the conversion of xanthotoxin into 5-
CC hydroxyxanthotoxin (PubMed:29971079). {ECO:0000269|PubMed:29971079,
CC ECO:0000303|PubMed:29971079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + xanthotoxin = 5-
CC hydroxyxanthotoxin + 2 H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:58064, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18358, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:78326; Evidence={ECO:0000269|PubMed:29971079};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58065;
CC Evidence={ECO:0000269|PubMed:29971079};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.3 uM for xanthotoxin (at pH 7.4 and 28 degrees Celsius)
CC {ECO:0000269|PubMed:29971079};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; MH000221; AXB38863.1; -; mRNA.
DR KEGG; ag:AXB38863; -.
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: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 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..506
FT /note="5-OH-xanthotoxin synthase"
FT /id="PRO_0000454521"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 365..370
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT BINDING 446
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 118
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT SITE 301
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT SITE 305
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
SQ SEQUENCE 506 AA; 57965 MW; 7E9BE6F86C579190 CRC64;
MDPVVIFLVL AFPIASVYLL FYHKKRVGGL SSPPGPRGLP FIGNFFQLYK APCIHEYLWN
LSKKYGSLMT LHMGSVPILV VSSPKMAKEV LKTQDLIYCS RPRMTGMRKL SYDGLDVAFS
TYSEHWRHVR KLCTLELFTQ KRAQLCFRLV HEQEVSRMIV RLSETAAASK DVNAFECFSN
LSTSIISRVA FGKRYDEDGI GKERLQRMLS EIDAMLAGIF VSDFFPMFGW IDRLSGMRAR
LDRTFKEMDM FYEELIDEHL KPNRPESPTE DLIDVMLKNK GSSCLLTMDS IKAILLNVFN
GGTGTSATLL VWAMTALMRN QGVMKKAQED IRRVIGRKGN VDEDDIQNLS YLRAVVKETM
RLYPTGPLLI PRETMESSII GEDKDHMYMI KPKTLVYVSM WAIGRDPEIW KNPMEFVPER
FLERPDLNYK GQQFEYIPFG AGRRICAGIH LGVTTVELAL ANLLYTFDWE PPAGTRFEDI
DDETLNGLTL QKKNALYIRP KKYICP
