GO_CATRO
ID GO_CATRO Reviewed; 501 AA.
AC I1TEM0;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Geissoschizine oxidase {ECO:0000303|PubMed:29511102};
DE Short=CrGO {ECO:0000303|PubMed:29511102};
DE EC=1.14.14.- {ECO:0000305|PubMed:29511102};
DE AltName: Full=Cytochrome P450 71AY2 {ECO:0000303|PubMed:24710322};
DE Short=CYP71AY2 {ECO:0000303|PubMed:24710322};
DE AltName: Full=Cytochrome P450 71D1V1 {ECO:0000303|PubMed:22837051};
DE Short=CYP71D1V1 {ECO:0000303|PubMed:22837051};
GN Name=GO {ECO:0000303|PubMed:29511102};
GN Synonyms=CYP71AY2 {ECO:0000303|PubMed:24710322},
GN CYP71D1V1 {ECO:0000303|PubMed:22837051};
GN ORFNames=Caros007686 {ECO:0000303|PubMed:24710322};
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].
RC STRAIN=cv. Wuhan Garden;
RX PubMed=22837051; DOI=10.1007/s00425-012-1712-0;
RA Huang L., Li J., Ye H., Li C., Wang H., Liu B., Zhang Y.;
RT "Molecular characterization of the pentacyclic triterpenoid biosynthetic
RT pathway in Catharanthus roseus.";
RL Planta 236:1571-1581(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Little Bright Eyes;
RX PubMed=24710322; DOI=10.1038/ncomms4606;
RA Miettinen K., Dong L., Navrot N., Schneider T., Burlat V., Pollier J.,
RA Woittiez L., van der Krol S., Lugan R., Ilc T., Verpoorte R.,
RA Oksman-Caldentey K.M., Martinoia E., Bouwmeester H., Goossens A.,
RA Memelink J., Werck-Reichhart D.;
RT "The seco-iridoid pathway from Catharanthus roseus.";
RL Nat. Commun. 5:3606-3606(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RX PubMed=29511102; DOI=10.1073/pnas.1719979115;
RA Qu Y., Easson M.E.A.M., Simionescu R., Hajicek J., Thamm A.M.K., Salim V.,
RA De Luca V.;
RT "Solution of the multistep pathway for assembly of corynanthean, strychnos,
RT iboga, and aspidosperma monoterpenoid indole alkaloids from 19E-
RT geissoschizine.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3180-3185(2018).
RN [4]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Little Delicata;
RX PubMed=30256480; DOI=10.1111/tpj.14111;
RA Qu Y., Safonova O., De Luca V.;
RT "Completion of the canonical pathway for assembly of anticancer drugs
RT vincristine/vinblastine in Catharanthus roseus.";
RL Plant J. 97:257-266(2019).
CC -!- FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid
CC indole alkaloids (MIAs, e.g. vincristine, quinine, and strychnine)
CC biosynthesis pathway. Catalyzes the oxidation of 19E-geissoschizine to
CC produce a short-lived MIA unstable intermediate which can be
CC spontaneously converted into akuammicine or oxidized by Redox1 and
CC Redox2 to produce stemmadenine and 16S/R-deshydroxymethylstemmadenine
CC (16S/R-DHS). {ECO:0000269|PubMed:29511102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(19S)-geissoschizine + O2 + reduced [NADPH--hemoprotein
CC reductase] = akuammicine + formate + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:58520, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17037,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142754;
CC Evidence={ECO:0000269|PubMed:29511102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58521;
CC Evidence={ECO:0000269|PubMed:29511102};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(19S)-geissoschizine + O2 + reduced [NADPH--hemoprotein
CC reductase] = 15alpha-stemmadenine intermediate I + 2 H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:58516, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17037, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:142668;
CC Evidence={ECO:0000269|PubMed:29511102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58517;
CC Evidence={ECO:0000269|PubMed:29511102};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29511102}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf epidermis (PubMed:24710322,
CC PubMed:30256480). Also present in the leaf internal phloem-associated
CC parenchyma (IPAP) inside the mesophyll (PubMed:24710322).
CC {ECO:0000269|PubMed:24710322, ECO:0000269|PubMed:30256480}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of catharanthine, vindoline and
CC ajmalicine, but accumulation of their precursor 19E-geissoschizine and
CC its derivatives pericyclivine and perivine.
CC {ECO:0000269|PubMed:29511102}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; JN613015; AEX07770.1; -; mRNA.
DR EMBL; KF302072; AHK60839.1; -; mRNA.
DR EMBL; MF770508; AVM85916.1; -; mRNA.
DR AlphaFoldDB; I1TEM0; -.
DR SMR; I1TEM0; -.
DR BioCyc; MetaCyc:MON-20645; -.
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 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 SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..501
FT /note="Geissoschizine oxidase"
FT /id="PRO_0000446410"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 442
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:P04798"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 501 AA; 57214 MW; 577CE560FF62B64B CRC64;
MEFSFSSPAL YIVYFLLFFV VRQLLKPKSK KKLPPGPRTL PLIGNLHQLS GPLPHRTLKN
LSDKHGPLMH VKMGERSAII VSDARMAKIV LHNNGLAVAD RSVNTVASIM TYNSLGVTFA
QYGDYLTKLR QIYTLELLSQ KKVRSFYSCF EDELDTFVKS IKSNVGQPMV LYEKASAYLY
ATICRTIFGS VCKEKEKMIK IVKKTSLLSG TPLRLEDLFP SMSIFCRFSK TLNQLRGLLQ
EMDDILEEII VEREKASEVS KEAKDDEDML SVLLRHKWYN PSGAKFRITN ADIKAIIFEL
ILAATLSVAD VTEWAMVEIL RDPKSLKKVY EEVRGICKEK KRVTGYDVEK MEFMRLCVKE
STRIHPAAPL LVPRECREDF EVDGYTVPKG AWVITNCWAV QMDPTVWPEP EKFDPERYIR
NPMDFYGSNF ELIPFGTGRR GCPGILYGVT NAEFMLAAMF YHFDWEIADG KKPEEIDLTE
DFGAGCIMKY PLKLVPHLVN D
