SLS_CATRO
ID SLS_CATRO Reviewed; 527 AA.
AC U5NDT8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Secologanin synthase {ECO:0000303|PubMed:24104568};
DE Short=CrSLS {ECO:0000303|PubMed:24104568};
DE EC=1.14.19.62 {ECO:0000269|PubMed:24104568};
DE AltName: Full=Cytochrome P450 72C {ECO:0000303|PubMed:24710322};
DE Short=CrCYP72C {ECO:0000303|PubMed:24710322};
GN Name=SLS {ECO:0000303|PubMed:24104568};
GN Synonyms=CYP72C {ECO:0000303|PubMed:24710322};
GN ORFNames=Caros020659 {ECO:0000305};
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, DISRUPTION
RP PHENOTYPE, PATHWAY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Little Delicata;
RX PubMed=24104568; DOI=10.1105/tpc.113.115154;
RA Asada K., Salim V., Masada-Atsumi S., Edmunds E., Nagatoshi M.,
RA Terasaka K., Mizukami H., De Luca V.;
RT "A 7-deoxyloganetic Acid glucosyltransferase contributes a key step in
RT secologanin biosynthesis in madagascar periwinkle.";
RL Plant Cell 25:4123-4134(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY JASMONIC ACID.
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. secologanin) biosynthesis pathway.
CC Catalyzes the conversion of loganin into secologanin.
CC {ECO:0000269|PubMed:24104568}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=loganin + O2 + reduced [NADPH--hemoprotein reductase] = H(+) +
CC 2 H2O + oxidized [NADPH--hemoprotein reductase] + secologanin;
CC Xref=Rhea:RHEA:20585, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15771, ChEBI:CHEBI:18002, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.19.62;
CC Evidence={ECO:0000269|PubMed:24104568};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:24104568}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves (especially in leaf epidermis),
CC and, to a lower extent, in roots, stems, flower buds and flowers.
CC {ECO:0000269|PubMed:24104568}.
CC -!- INDUCTION: By jasmonic acid (MeJA). {ECO:0000269|PubMed:24710322}.
CC -!- DISRUPTION PHENOTYPE: Large increases in loganin accumulation.
CC {ECO:0000269|PubMed:24104568}.
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; KF415117; AGX93064.1; -; mRNA.
DR EMBL; KF309242; AHK60848.1; -; mRNA.
DR AlphaFoldDB; U5NDT8; -.
DR SMR; U5NDT8; -.
DR BRENDA; 1.14.19.62; 1211.
DR BRENDA; 1.3.3.9; 1211.
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:0050616; F:secologanin synthase activity; IDA:UniProtKB.
DR GO; GO:0009820; P: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 Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..527
FT /note="Secologanin synthase"
FT /id="PRO_0000446409"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 470
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 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 527 AA; 61055 MW; BAAB1FECD1787612 CRC64;
MEMDMDIIRK AIAATIFALV MAWAWRVLDW AWFTPKRIEK RLRQQGFRGN PYRFLVGDVK
ESGKMHQEAL SNPMEFDNDI VPRLMPHINH TIKTYGRNSF TWMGRIPRIH VMEPELIKEV
LTHSSKYQKN FDVHNPLVKF LLTGVGSFEG AKWSKHRRII SPAFTLEKLK SMLPAFAICY
HDMLTKWEKL AEKEGSHEVD IFPTFDVLTS DVISKVAFGS TYDEGGKIFR LLKELMDLTI
DCMRDVYIPG WSYLPTKRNK RMKEINKEIT DMLRFIINKR MKALKAGEPG EDDLLGVLLE
SNIQEIQKQG NRKDGGMTIN DVIEECKLFY FAGQETTGVL LTWTTILLSK HPEWQERARE
EVLQAFGKNK PEFERLNHLK YVSMILYEVL RLYPPVIDLT KIIHEDTKLG PYTIPAGTQV
MLPTVMLHRE KSIWGEDAME FNPMRFADGV ANATKNNVTY LPFSWGPRVC LGQNFALLQA
KLGLAMILQR FKFDVAPSYV HAPFTILTVQ PQFGSHVIYK KLERQNF
