IO_CATRO
ID IO_CATRO Reviewed; 515 AA.
AC W8JIS5;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Iridoid oxidase {ECO:0000303|PubMed:24710322};
DE Short=CrIO {ECO:0000303|PubMed:24710322};
DE EC=1.14.14.161 {ECO:0000269|PubMed:24710322};
DE AltName: Full=Cytochrome P450 76A26 {ECO:0000303|PubMed:24710322};
DE Short=CrCYP76A26 {ECO:0000303|PubMed:24710322};
GN Name=IO {ECO:0000303|PubMed:24710322};
GN Synonyms=CYP76A26 {ECO:0000303|PubMed:24710322};
GN ORFNames=Caros003676 {ECO:0000305},
GN Caros020058 {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], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION BY JASMONIC ACID, PATHWAY, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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).
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 conversion of cis-trans-
CC nepetalactol (iridodial) into 7-deoxyloganetic acid. Converts also
CC iridotrial into 7-deoxyloganetic acid. {ECO:0000269|PubMed:24710322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-cis-trans-nepetalactol + 3 O2 + 3 reduced [NADPH--
CC hemoprotein reductase] = 7-deoxyloganetate + 4 H(+) + 4 H2O + 3
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57560,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:26,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76846;
CC EC=1.14.14.161; Evidence={ECO:0000269|PubMed:24710322};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57561;
CC Evidence={ECO:0000269|PubMed:24710322};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 5.2 sec(-1) with cis-trans-nepetalactol as substrate.
CC {ECO:0000269|PubMed:24710322};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:24710322}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24710322}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the leaf internal phloem-associated
CC parenchyma (IPAP) inside the mesophyll. {ECO:0000269|PubMed:24710322}.
CC -!- INDUCTION: By jasmonic acid (MeJA). {ECO:0000269|PubMed:24710322}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=ORCAE database;
CC URL="https://bioinformatics.psb.ugent.be/orcae/overview/Catro";
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DR EMBL; KF302066; AHK60833.1; -; mRNA.
DR AlphaFoldDB; W8JIS5; -.
DR SMR; W8JIS5; -.
DR BioCyc; MetaCyc:MON-20520; -.
DR BRENDA; 1.14.14.161; 1211.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0035834; P:indole alkaloid metabolic process; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; 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 Alkaloid metabolism; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..515
FT /note="Iridoid oxidase"
FT /id="PRO_0000446407"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 455
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"
SQ SEQUENCE 515 AA; 58748 MW; 3B4443A1A1AC4F19 CRC64;
MATITFDSLN PVTVAISAGF LLLLIIFVKS RTGSSKRKPP GPPGWPIFGN MFDLGDLPHQ
TLYKLKSKYG PIVWLQLGSI NTMVVQNAVS AAELFKKHDV PFCDRKVPDT LTAFNFNQGS
LGMNTYGGHW RVLRRLCSME FLVNKRMNET TDLRRRIEDN MVRWIEEDSL ASKAQGGTGA
VQLSRFLFLM AFNLVGNLML SRDLMDNKDP EGREFFDCMN EILELAGTPN IADFLPLLKK
LDPLGMKKRM VDNMSRTMKI SSKFVQERLD NRKAGKINEK KDFLDVMLEY QGDGKDGPDK
FTEQHVNIVI MEMFFAGSET TSISIEWGFT ELLRNPHAFK KVREEIDRVV GVNRMVEETD
MENLPYLQAV VKETLRLHPA LPMLLPRNTM EDTEYMGYLI PKGTQVFVNA WAIGRDPEYW
QDPLSFKPER FINSSVEYKG QHFELIPFGS GRRICVGFPL AHRVVHLTLA TLVQAFDWDL
GAGVKPQDID LEERLGLTLR KKNPLNVIPK KRVHI
