TEX1_CATRO
ID TEX1_CATRO Reviewed; 506 AA.
AC A0A343URW6;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Tabersonine 6,7-epoxidase isoform 1 {ECO:0000303|PubMed:29934299, ECO:0000303|PubMed:31009114};
DE EC=1.14.14.- {ECO:0000269|PubMed:29934299, ECO:0000269|PubMed:31009114};
DE AltName: Full=Cytochrome P450 71D521 {ECO:0000303|PubMed:29934299, ECO:0000303|PubMed:31009114};
GN Name=TEX1 {ECO:0000303|PubMed:29934299, ECO:0000303|PubMed:31009114};
GN Synonyms=CYP71D521 {ECO:0000303|PubMed:29934299,
GN ECO:0000303|PubMed:31009114};
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=29934299; DOI=10.1104/pp.18.00549;
RA Carqueijeiro I.T., Brown S., Chung K., Dang T.-T., Walia M., Besseau S.,
RA Duge de Bernonville T., Oudin A., Lanoue A., Billet K., Munsch T.,
RA Koudounas K., Melin C., Godon C., Razafimandimby B., de Craene J.-O.,
RA Glevarec G., Marc J., Giglioli-Guivarc'h N., Clastre M., St-Pierre B.,
RA Papon N., Andrade R.B., O'Connor S.E., Courdavault V.;
RT "Two tabersonine 6,7-epoxidases initiate lochnericine-derived alkaloid
RT biosynthesis in Catharanthus roseus.";
RL Plant Physiol. 177:1473-1486(2018).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=31009114; DOI=10.1111/tpj.14346;
RA Williams D., Qu Y., Simionescu R., De Luca V.;
RT "The assembly of (+)-vincadifformine- and (-)-tabersonine-derived
RT monoterpenoid indole alkaloids in Catharanthus roseus involves separate
RT branch pathways.";
RL Plant J. 99:626-636(2019).
CC -!- FUNCTION: Component of the monoterpenoid indole alkaloids (MIAs, e.g.
CC echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and
CC horhammericine) biosynthetic pathway; MIAs are used in cancer treatment
CC and other medical applications (PubMed:31009114). Cytochrome P450
CC catalyzing the conversion of tabersonine to lochnericine
CC (PubMed:31009114, PubMed:29934299). {ECO:0000269|PubMed:29934299,
CC ECO:0000269|PubMed:31009114}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-tabersonine + O2 + reduced [NADPH--hemoprotein reductase]
CC = H(+) + H2O + lochnericine + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:61056, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:57893, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:144374; Evidence={ECO:0000269|PubMed:29934299,
CC ECO:0000269|PubMed:31009114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61057;
CC Evidence={ECO:0000269|PubMed:29934299, ECO:0000269|PubMed:31009114};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.08 uM for tabersonine (at pH 8.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:29934299};
CC Vmax=0.254 pmol/sec/ug enzyme with tabersonine as substrate (at pH
CC 8.4 and 30 degrees Celsius) {ECO:0000269|PubMed:29934299};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:31009114}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:29934299}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots.
CC {ECO:0000269|PubMed:29934299}.
CC -!- DISRUPTION PHENOTYPE: Decreased lochnericine production, but increased
CC tabersonine accumulation. {ECO:0000269|PubMed:29934299}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; MG873080; AVH80640.1; -; mRNA.
DR AlphaFoldDB; A0A343URW6; -.
DR SMR; A0A343URW6; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0035835; P:indole alkaloid 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 Alkaloid metabolism; Endoplasmic reticulum; Glycoprotein; Heme; Iron;
KW Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..506
FT /note="Tabersonine 6,7-epoxidase isoform 1"
FT /id="PRO_5016633182"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 441
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:Q96242"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 506 AA; 57513 MW; 8F3C9ECCDA609D21 CRC64;
MEFVVSLFAF VVSCFILLKV AKNSKNPKRN TNLELPPGPK QLPIIGNLHQ LGGGLAHHVL
RNLGKQYGPL MHLKIGELST IVVSSTEIAK EVFKTHDIHF SNRPSHILVF KIVSYDYKDI
VLSQYGKYWR ELRKVCNLEL LSPNRVQSFR SIREDAVLNM MKSISSNDGK VVNLSEMILS
LIYGITARAA FGVWSKKHEE FIRLESEIQR LATTFVLADM FPSIKFLGAL SGLRYKVEKV
HKKVDDILEG ILKEHRRQNN NMTEENGKKD LVDVLLNIQK NGDMETPFTD QHIKAIIFDM
FSAGTLTSTI AVDWAMAEMM KNPSVLKRAQ DEVRNVYNGI GNVDESKLDE LKYLQAVIKE
TLRIHPGTPI VHRETREECE INGYRIPAKA RVMVNAWAIS RDPNYWPEPD IFKPERFLGS
EVDFKGTHFE YIPFGAGRRI CPGISYAIAN VQLPLAQLLY HFEWKLPGGM KPEELDMTEI
LGTAAQRKEN LLLIPNSHSC SSLKQV
