7DLH_CATRO
ID 7DLH_CATRO Reviewed; 521 AA.
AC U5NE19;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=7-deoxyloganic acid hydroxylase {ECO:0000303|PubMed:24103035, ECO:0000303|PubMed:24710322};
DE Short=Cr7DLH {ECO:0000303|PubMed:24103035, ECO:0000303|PubMed:24710322};
DE EC=1.14.14.85 {ECO:0000269|PubMed:24103035, ECO:0000269|PubMed:24710322};
DE AltName: Full=Cytochrome P450 72A224 {ECO:0000303|PubMed:24710322};
DE Short=CYP72A224 {ECO:0000303|PubMed:24710322};
GN Name=7DLH {ECO:0000303|PubMed:24103035, ECO:0000303|PubMed:24710322};
GN Synonyms=CYP72A224 {ECO:0000303|PubMed:24710322};
GN ORFNames=Caros005234 {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, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=24103035; DOI=10.1111/tpj.12330;
RA Salim V., Yu F., Altarejos J., De Luca V.;
RT "Virus-induced gene silencing identifies Catharanthus roseus 7-deoxyloganic
RT acid-7-hydroxylase, a step in iridoid and monoterpene indole alkaloid
RT biosynthesis.";
RL Plant J. 76:754-765(2013).
RN [2]
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 7-deoxyloganic acid
CC into loganic acid (PubMed:24710322, PubMed:24103035). Not active on 7-
CC deoxyloganetic acid (PubMed:24710322). {ECO:0000269|PubMed:24103035,
CC ECO:0000269|PubMed:24710322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-deoxyloganate + O2 + reduced [NADPH--hemoprotein reductase]
CC = H(+) + H2O + loganate + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:57576, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18052, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76844; EC=1.14.14.85;
CC Evidence={ECO:0000269|PubMed:24103035, ECO:0000269|PubMed:24710322};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57577;
CC Evidence={ECO:0000269|PubMed:24103035, ECO:0000269|PubMed:24710322};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=111 uM for 7-deoxyloganic acid {ECO:0000269|PubMed:24103035};
CC KM=30 uM for NADPH {ECO:0000269|PubMed:24103035};
CC Vmax=5.5 umol/min/ug enzyme with 7-deoxyloganic acid as substrate
CC {ECO:0000269|PubMed:24103035};
CC Vmax=4.19 umol/min/ug enzyme with NADPH as substrate
CC {ECO:0000269|PubMed:24103035};
CC Vmax=0.01 pmol/sec/mg enzyme with 7-deoxyloganic acid 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}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly present in actively growing aerial organs,
CC including leaves, flower buds and stems, and, to a lower extent, in
CC mature leaves, roots and opened flowers (PubMed:24103035). Expressed in
CC the leaf internal phloem-associated parenchyma (IPAP) inside the
CC mesophyll (PubMed:24710322). {ECO:0000269|PubMed:24103035,
CC ECO:0000269|PubMed:24710322}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in young leave and fades
CC out during aging. {ECO:0000269|PubMed:24103035}.
CC -!- INDUCTION: By jasmonic acid (MeJA). {ECO:0000269|PubMed:24710322}.
CC -!- DISRUPTION PHENOTYPE: Reduced secologanin levels but accumulation of 7-
CC deoxyloganic acid. {ECO:0000269|PubMed:24103035}.
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; KF415115; AGX93062.1; -; mRNA.
DR EMBL; KF302067; AHK60834.1; -; mRNA.
DR AlphaFoldDB; U5NE19; -.
DR SMR; U5NE19; -.
DR KEGG; ag:AHK60834; -.
DR BioCyc; MetaCyc:MON-20522; -.
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:0050595; F:7-deoxyloganin 7-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0035834; P:indole alkaloid metabolic process; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; 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; Glycoprotein; Heme; Iron; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..521
FT /note="7-deoxyloganic acid hydroxylase"
FT /id="PRO_0000446408"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 469
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 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 521 AA; 60022 MW; 20BD06F9DDBFBDE1 CRC64;
MELNFKSIIF LVFVSLTLYW VYRILDWVWF KPKKLEKCLR EQGFKGNPYR LFLGDQYDSG
KLIRQALTKP IGVEEDVKKR IVPHILKTVG THGKKSFMWV GRIPRVNITD PELIKEVLTK
YYKFQKNHHD LDPITKLLLT GIGSLEGDPW AKRRKIINAA FHFEKLKLML PAFYLSCRDM
VTKWDNKVPE GGSAEVDVWH DIETLTGDVI SRTLFGSNFE EGRRIFELMK ELTALTIDVI
RSVYIPGQRF LPTKRNNRMR AIDKEVRVRI TEIINKKMKV MKSGEAASAA DDFLGILLEC
NLNEIKEQGN NKSAGMTIGE IIGECKLFYF AGQDTTSTLL VWTMVLLSRF PEWQTRAREE
VFQVFGNKTP DYDGISHLKV ITMILYEVLR LYTPVAELTK VAHEATQLGK YFIPAGVQLM
MPQILLHHDP EIWGEDVMEF KPERFAEGVL KATKSQGSFF PFSLGPRMCI GQNFALLEAK
MAMSLILRRF SFELSPSYVH APFTLITMQP QYGAHLILHK L
