LAMT_CATRO
ID LAMT_CATRO Reviewed; 371 AA.
AC B2KPR3;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Loganic acid O-methyltransferase {ECO:0000303|PubMed:24104568, ECO:0000303|PubMed:29399933};
DE Short=CrLAMT {ECO:0000303|PubMed:24104568, ECO:0000303|PubMed:29399933};
DE EC=2.1.1.50 {ECO:0000269|PubMed:18326827, ECO:0000269|PubMed:24104568, ECO:0000269|PubMed:29399933};
GN Name=LAMT {ECO:0000303|PubMed:24104568, ECO:0000303|PubMed:29399933};
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, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP PATHWAY.
RC STRAIN=cv. Little Delicata; TISSUE=Leaf;
RX PubMed=18326827; DOI=10.1105/tpc.107.056630;
RA Murata J., Roepke J., Gordon H., De Luca V.;
RT "The leaf epidermome of Catharanthus roseus reveals its biochemical
RT specialization.";
RL Plant Cell 20:524-542(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, 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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND LOGANIC ACID, FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF TYR-31; TYR-37; GLN-38; TYR-159; HIS-162; TRP-163; HIS-245;
RP GLN-273 AND GLN-316, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29399933; DOI=10.1002/cbic.201700679;
RA Petronikolou N., Hollatz A., Schuler M.A., Nair S.K.;
RT "Loganic acid methyltransferase: Insights into the specificity of
RT methylation on an iridoid glycoside.";
RL ChemBioChem 19:784-788(2018).
CC -!- FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid
CC indole alkaloids (MIAs, e.g. vinblastine and ajmalicine) biosynthesis
CC pathway. Catalyzes the methylation of loganic acid (6S,7R) to produce
CC loganin (PubMed:29399933, PubMed:18326827, PubMed:24104568). Weak
CC activity with secologanic acid as substrate. Inactive on deoxyloganic,
CC dehydrologanic, epiloganic and loganetic acid (PubMed:18326827).
CC {ECO:0000269|PubMed:18326827, ECO:0000269|PubMed:24104568,
CC ECO:0000269|PubMed:29399933}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=loganate + S-adenosyl-L-methionine = loganin + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:12508, ChEBI:CHEBI:15771,
CC ChEBI:CHEBI:18052, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.50;
CC Evidence={ECO:0000269|PubMed:18326827, ECO:0000269|PubMed:24104568,
CC ECO:0000269|PubMed:29399933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12509;
CC Evidence={ECO:0000269|PubMed:18326827};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLN8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8};
CC -!- ACTIVITY REGULATION: Strongly repressed by loganin and slightly by S-
CC adenosyl-L-homocysteine. {ECO:0000269|PubMed:18326827}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=315 uM for loganic acid (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:29399933};
CC KM=15 mM for loganic acid {ECO:0000269|PubMed:18326827};
CC KM=742 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18326827};
CC Note=kcat is 0.31 sec(-1) with loganic acid as substrate (at pH 7.5
CC and 30 degrees Celsius). {ECO:0000269|PubMed:29399933};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:18326827};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:18326827,
CC ECO:0000269|PubMed:24104568}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9FLN8}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves (especially in leaf epidermis),
CC flowers, siliques and stems, and, at low levels, in hairy roots.
CC {ECO:0000269|PubMed:18326827, ECO:0000269|PubMed:24104568}.
CC -!- DISRUPTION PHENOTYPE: Large increases in loganic acid accumulation.
CC {ECO:0000269|PubMed:24104568}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase 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; EU057974; ABW38009.1; -; mRNA.
DR EMBL; KF415116; AGX93063.1; -; mRNA.
DR PDB; 6C8R; X-ray; 1.95 A; A/B=1-371.
DR PDB; 6C8S; X-ray; 2.20 A; A/B=1-371.
DR PDBsum; 6C8R; -.
DR PDBsum; 6C8S; -.
DR AlphaFoldDB; B2KPR3; -.
DR SMR; B2KPR3; -.
DR MINT; B2KPR3; -.
DR BioCyc; MetaCyc:MON-13907; -.
DR BRENDA; 2.1.1.50; 1211.
DR GO; GO:0030749; F:loganate O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035834; P:indole alkaloid metabolic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..371
FT /note="Loganic acid O-methyltransferase"
FT /id="PRO_0000446406"
FT BINDING 31
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 34..38
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 77..78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 112..115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 141..143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 158..160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 159..163
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 240..245
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29399933,
FT ECO:0007744|PDB:6C8R, ECO:0007744|PDB:6C8S"
FT MUTAGEN 31
FT /note="Y->F: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:29399933"
FT MUTAGEN 37
FT /note="Y->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:29399933"
FT MUTAGEN 38
FT /note="Q->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:29399933"
FT MUTAGEN 159
FT /note="Y->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:29399933"
FT MUTAGEN 162
FT /note="H->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:29399933"
FT MUTAGEN 163
FT /note="W->F: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:29399933"
FT MUTAGEN 245
FT /note="H->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:29399933"
FT MUTAGEN 273
FT /note="Q->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:29399933"
FT MUTAGEN 316
FT /note="Q->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:29399933"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 36..56
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:6C8R"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:6C8R"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6C8R"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:6C8R"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:6C8R"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 191..215
FT /evidence="ECO:0007829|PDB:6C8R"
FT STRAND 216..227
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 240..257
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:6C8R"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:6C8R"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 310..329
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:6C8R"
FT HELIX 349..354
FT /evidence="ECO:0007829|PDB:6C8R"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:6C8R"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:6C8R"
SQ SEQUENCE 371 AA; 42018 MW; 031EB28DCF308B08 CRC64;
MVATIDSIEM PALPTAVEAH PMKGGDDSHS YSQNSCYQKG VIDAAKAVIV EAVNEKLDLE
NNPIFDPIKP FRIADFGCST GPNTFHAMQN IVESVETKYK SLQKTPEFHV FFNDHVNNDF
NVLFRSLPPN REFFAAGVPG SFYTRVFPKN SIHFAHCSYA LHWLSKVPKE IQDKNSLAYN
KGRIHYTGTE KHVVKAYFGQ FQRDFEGFLK ARAQEIVVGG LMVIQIPGLP SGEVLFSRTG
AGLLHFLLGT SLMELVNKGI INEESVDSFN LPQYHPSVED LEMVIEMNDC FTIERVGTLP
HPMKNLPFDV QRTSLQVRAI MECILTEHFG ENILDPLFEI YTKNLQENFH VFDKEIRKDA
DLYLVLKRKG N
