C71Z1_AMMMJ
ID C71Z1_AMMMJ Reviewed; 509 AA.
AC D2CGS0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 30.
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 CYP71AZ1 {ECO:0000303|PubMed:29971079};
GN Name=CYP71AZ1 {ECO:0000303|PubMed:29971079};
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 [GENOMIC DNA].
RA Kellner S., Matern U.;
RT "Cytochrome P450-dependent monooxygenases of the furanocoumarin
RT biosynthesis from Ammi majus L.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REVIEW, AND
RP PATHWAY.
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=13.1 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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; EF127863; ABO32529.1; -; Genomic_DNA.
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 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..509
FT /note="5-OH-xanthotoxin synthase"
FT /id="PRO_0000454522"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 368..373
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT BINDING 449
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 120
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT SITE 304
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
FT SITE 308
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:A0A2Z5D850"
SQ SEQUENCE 509 AA; 58279 MW; B1EDA413E5C44F46 CRC64;
MQMDAVVILL ILAFPIASVY VLFYHKKRVD GLSEPPGPPG LPFIGNFYQL YKAPCIHEYL
CTLSKRYGSL MTLRMGSVPI LVVSSPKMAK EVLKTQDLAY CSRPMMTGMQ KLSYNGLDVA
FSPYSEHWRQ VRKFCTLELF TQKRAQIDFR HVHEQEVSRM IARLSETAAA SKDVNAFECF
SNLATSIISR VAFGKRHDED GIGKERLQRM LSELDTMLSV YFVSDFFPMF GWIDSLTGMR
ARLDRTFKEM DMFYEELIDD HLKPDRPESL TEDIIDVMLK NKGCSSSSLT KDTMKAILLN
VFNGGTGTSA SLLVWAMTAL MRNRGVMKKV QEEIRSVIGK KGNVDEDDIQ NLPYLRAVVK
ETMRLYPTGA LLIPRKTIES SIIGEDKDHM YMIKPKTLVY VSMWAIGRDP EIWKNPMKFV
PERFLERHDI NYQGQQFEYI PFGAGRRICP GIHLGLTTVE LALANLLYTF NWEPPVGTRF
EDINDETVNG ITLQKKNALY IRPKTYMFS
