HTOMT_CATRO
ID HTOMT_CATRO Reviewed; 355 AA.
AC B0EXJ8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Tabersonine 16-O-methyltransferase {ECO:0000303|PubMed:18053006};
DE EC=2.1.1.94 {ECO:0000269|PubMed:18053006};
GN Name=16OMT {ECO:0000303|PubMed:18053006};
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,
RP BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=18053006; DOI=10.1111/j.1365-313x.2007.03337.x;
RA Levac D.E., Murata J., Kim W.S., De Luca V.;
RT "Application of carborundum abrasion for investigating the leaf epidermis:
RT molecular cloning of Catharanthus roseus 16-hydroxytabersonine-16-O-
RT methyltransferase.";
RL Plant J. 53:225-236(2008).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16262708; DOI=10.1111/j.1365-313x.2005.02557.x;
RA Murata J., De Luca V.;
RT "Localization of tabersonine 16-hydroxylase and 16-OH tabersonine-16-O-
RT methyltransferase to leaf epidermal cells defines them as a major site of
RT precursor biosynthesis in the vindoline pathway in Catharanthus roseus.";
RL Plant J. 44:581-594(2005).
RN [3]
RP TISSUE SPECIFICITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21047699; DOI=10.1016/j.jplph.2010.08.018;
RA Guirimand G., Guihur A., Poutrain P., Hericourt F., Mahroug S.,
RA St-Pierre B., Burlat V., Courdavault V.;
RT "Spatial organization of the vindoline biosynthetic pathway in Catharanthus
RT roseus.";
RL J. Plant Physiol. 168:549-557(2011).
RN [4]
RP INDUCTION BY HERBIVORY.
RX PubMed=28094274; DOI=10.1038/srep40453;
RA Duge de Bernonville T., Carqueijeiro I., Lanoue A., Lafontaine F.,
RA Sanchez Bel P., Liesecke F., Musset K., Oudin A., Glevarec G., Pichon O.,
RA Besseau S., Clastre M., St-Pierre B., Flors V., Maury S., Huguet E.,
RA O'Connor S.E., Courdavault V.;
RT "Folivory elicits a strong defense reaction in Catharanthus roseus:
RT metabolomic and transcriptomic analyses reveal distinct local and systemic
RT responses.";
RL Sci. Rep. 7:40453-40453(2017).
CC -!- FUNCTION: 16-O-methyltransferase involved in the biosynthesis of
CC vindoline. Highly specific for 16-hydroxytabersonine. No activity with
CC tabersonine, 3-hydroxytyramine, 4-hydroxytyramine, 5-hydroxytryptamine
CC (5HT), 2,3-dihydro-3-hydroxytabersonine, lochnericine, hoerhammericine,
CC 16-hydroxy-2,3-dihydro-3-hydroxytabersonine, 16-hydroxylochnericine,
CC 16-hydroxyhoerhammericine, quercetin, kaempferol and caffeic acid as
CC substrates. {ECO:0000269|PubMed:18053006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16-hydroxytabersonine + S-adenosyl-L-methionine = 16-
CC methoxytabersonine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:20992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:58239, ChEBI:CHEBI:58930, ChEBI:CHEBI:59789; EC=2.1.1.94;
CC Evidence={ECO:0000269|PubMed:18053006};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for 16-hydroxytabersonine {ECO:0000269|PubMed:18053006};
CC KM=21.7 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18053006};
CC Vmax=0.58 mmol/sec/mg enzyme toward 16-hydroxytabersonine
CC {ECO:0000269|PubMed:18053006};
CC Vmax=0.79 mmol/sec/mg enzyme toward S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:18053006};
CC pH dependence:
CC Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:18053006};
CC -!- PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21047699}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21047699}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers. Detected in stems
CC and roots. In leaves, expressed in epidermal cells.
CC {ECO:0000269|PubMed:16262708, ECO:0000269|PubMed:18053006,
CC ECO:0000269|PubMed:21047699}.
CC -!- DEVELOPMENTAL STAGE: Peak of expression in 8-day-old seedlings. Highest
CC expression in the youngest leaf pair. {ECO:0000269|PubMed:18053006}.
CC -!- INDUCTION: Up-regulated by herbivory. {ECO:0000269|PubMed:28094274}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000305}.
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DR EMBL; EF444544; ABR20103.1; -; mRNA.
DR AlphaFoldDB; B0EXJ8; -.
DR SMR; B0EXJ8; -.
DR KEGG; ag:ABR20103; -.
DR BioCyc; MetaCyc:MON-12359; -.
DR BRENDA; 2.1.1.94; 1211.
DR UniPathway; UPA00365; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030766; F:11-O-demethyl-17-O-deacetylvindoline O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009821; P:alkaloid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF08100; Dimerisation; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..355
FT /note="Tabersonine 16-O-methyltransferase"
FT /id="PRO_0000412068"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 198..201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 222..223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 222
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 242..243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 355 AA; 39863 MW; 76E6CB586E427CA5 CRC64;
MDVQSEEFRG AQAQIWSQSC SFITSASLKC AVKLGIPDTI DNHGKPITLS ELTNALVPPV
HPSKAPFIYR LMRVLAKNGF CSEEQLDGET EPLYSLTPSS RILLKKEPLN LRGIVLTMAD
PVQLKAWESL SDWYQNEDDS STAFETAHGK NFWGYSSEHM EHAEFFNEAM ASDSQLISKL
LIGEYKFLFE GLASLVDIGG GTGTIAKAIA KNFPQLKCTV FDLPHVVANL ESKENVEFVA
GDMFEKIPSA NAIFLKWILH DWNDEDCVKI LKSCKKAIPA KGGKVIIIDM VMYSDKKDDH
LVKTQTSMDM AMLVNFAAKE RCEKEWAFLF KEAGFSDYKI YPKLDFTRSL IEVYP
