TEX2_CATRO
ID TEX2_CATRO Reviewed; 515 AA.
AC A0A343URW7;
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 2 {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 71D347 {ECO:0000303|PubMed:29934299, ECO:0000303|PubMed:31009114};
GN Name=TEX2 {ECO:0000303|PubMed:29934299, ECO:0000303|PubMed:31009114};
GN Synonyms=CYP71D347 {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, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND 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=6.45 uM for tabersonine (at pH 8.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:29934299};
CC Vmax=0.108 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 aerial organs, including stems,
CC leaves and flowers. {ECO:0000269|PubMed:29934299}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; MG873081; AVH80641.1; -; mRNA.
DR AlphaFoldDB; A0A343URW7; -.
DR SMR; A0A343URW7; -.
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..515
FT /note="Tabersonine 6,7-epoxidase isoform 2"
FT /id="PRO_0000448558"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
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:Q96242"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 515 AA; 58906 MW; AA105A64D509FB04 CRC64;
MEFVVSPFAF LIFFFILLKM IAKNFKNPKK NTKPLPPGPK KLPIIGNLHQ LGGGLAHHIL
RDLSQNYGPL MHLKIGELST IVISSTEMAK QVFKVHDIHF SNRPSHILVF KIVSYDYKDI
VLSQYGNYWR ELRKVCNLHL LSPNRVQSFR FIREDSVLNM MKSISSNEGK VVNLSEMILS
LIYGITARAA FGVWSKRHEE FIRLESEIQR LATTFVLADM FPSIKILGAL SGLRYKVEKV
HKKVDEILED ILKEHRNNNI SIEKEEEEEE ENNGGKKDLV DVLLDIQKNG EMETPFTDQH
IKAIIFDMFS AGTLTSTIAV DWAMAEMMKN PRVMKRAQEE VRNVYNGIGN VNESKLDELK
YLQAIIKETL RIHPGTPIVH RETREECEIN GYRIPAKARV MVNAWAISRD PNYWPDPDSF
KPERFLGSEV DFKGTHFEYT PFGAGRRICP GISYAIANIQ LPLAQLLYHF DWKLAGGMKP
EELDMAEILG TAAQRKEDLL LIPNSHSCSS LKQQV
