PMT1_NICAT
ID PMT1_NICAT Reviewed; 388 AA.
AC Q93XQ5;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Putrescine N-methyltransferase 1 {ECO:0000303|PubMed:11299398};
DE Short=NaPMT1 {ECO:0000303|PubMed:11299398};
DE EC=2.1.1.53 {ECO:0000255|PROSITE-ProRule:PRU00947};
GN Name=PMT1 {ECO:0000303|PubMed:11299398};
OS Nicotiana attenuata (Coyote tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=49451;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY JASMONATE; WOUNDING AND
RP MANDUCA SEXTA.
RC TISSUE=Root;
RX PubMed=11299398; DOI=10.1104/pp.125.4.2189;
RA Winz R.A., Baldwin I.T.;
RT "Molecular interactions between the specialist herbivore Manduca sexta
RT (Lepidoptera, Sphingidae) and its natural host Nicotiana attenuata. IV.
RT Insect-Induced ethylene reduces jasmonate-induced nicotine accumulation by
RT regulating putrescine N-methyltransferase transcripts.";
RL Plant Physiol. 125:2189-2202(2001).
RN [2]
RP REVIEW ON PUTRESCINE N-METHYLTRANSFERASE.
RX PubMed=19651420; DOI=10.1016/j.phytochem.2009.06.012;
RA Biastoff S., Brandt W., Draeger B.;
RT "Putrescine N-methyltransferase--the start for alkaloids.";
RL Phytochemistry 70:1708-1718(2009).
RN [3]
RP TISSUE SPECIFICITY, AND REVIEW ON NICOTINE BIOSYNTHESIS.
RX PubMed=28536194; DOI=10.1073/pnas.1700073114;
RA Xu S., Brockmoeller T., Navarro-Quezada A., Kuhl H., Gase K., Ling Z.,
RA Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA Timmermann B., Gaquerel E., Baldwin I.T.;
RT "Wild tobacco genomes reveal the evolution of nicotine biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6133-6138(2017).
CC -!- FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural
CC products, leading mainly to the production of anabasine, anatabine,
CC nicotine and nornicotine, effective deterrents against herbivores with
CC antiparasitic and pesticide properties (neurotoxins); nornicotine
CC serves as the precursor in the synthesis of the carcinogen compound N'-
CC nitrosonornicotine (NNN) (By similarity). Methyltransferase that
CC mediates the conversion of putrescine to N-methylputrescine (By
CC similarity). {ECO:0000250|UniProtKB:Q42963}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=putrescine + S-adenosyl-L-methionine = H(+) + N-
CC methylputrescine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15037,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58039,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:326268; EC=2.1.1.53;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00947};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000250|UniProtKB:Q42963}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots.
CC {ECO:0000269|PubMed:28536194}.
CC -!- INDUCTION: Triggered by jasmonic acid (MeJA); this induction is
CC repressed by 2-chloroethylphosphonic acid (ethephon), an ethylene
CC precursor, that can by alleviated by 1-methylcyclopropene (1-MCP), a
CC competitive inhibitor of ethylene receptors (PubMed:11299398).
CC Accumulates upon wounding and feeding by the specialist herbivore
CC Manduca sexta; these induction is dramatically amplified by a
CC pretreatment with 1-MCP (PubMed:11299398).
CC {ECO:0000269|PubMed:11299398}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Spermidine/spermine synthase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00947}.
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DR EMBL; AF280402; AAK49870.1; -; mRNA.
DR BRENDA; 2.1.1.53; 9729.
DR UniPathway; UPA00107; -.
DR GO; GO:0030750; F:putrescine N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009625; P:response to insect; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR Gene3D; 2.30.140.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00198; Spermidine_synth; 1.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR030373; PABS_CS.
DR InterPro; IPR025803; Putrescine_N-MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR InterPro; IPR035246; Spermidine_synt_N.
DR InterPro; IPR037163; Spermidine_synt_N_sf.
DR PANTHER; PTHR11558; PTHR11558; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00417; speE; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
DR PROSITE; PS51615; SAM_MT_PUTRESCINE; 1.
PE 2: Evidence at transcript level;
KW Alkaloid metabolism; Methyltransferase; Polyamine biosynthesis;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..388
FT /note="Putrescine N-methyltransferase 1"
FT /id="PRO_0000455796"
FT DOMAIN 99..336
FT /note="PABS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00354"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00354,
FT ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 205
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 236..237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
SQ SEQUENCE 388 AA; 42627 MW; 413E8C1745BA2925 CRC64;
MEVISTNTNG STIFKNGAIP MNGYQNGTSK HQNGHQNGTS EHRNGHQNGI SEHQNGHKNG
TSEHQNGHQN GTSEQQNGTI SHDNGNELQL LGSSNSIKPG WFSEFSALWP GEAFSLKVEK
LLFQGKSDYQ DVMLFESATY GKVLTLDGAI QHTENGGFPY TEMIVHLPLG SIPNPKKVLI
IGGGIGFTLF EMLRYPSIEK IDIVEIDDVV VDVSRKFFPY LAANFNDPRV TLVLGDGAAF
VKAAQAGYYD AIIVDSSDPI GPAKDLFERP FFEAVAKALR PGGVVCTQAE SIWLHMHIIK
QIIANCRQVF KGSVNYAWTT VPTYPTGVIG YMLCSTEGPE VDFKNPINPI DKETTQVKSK
LAPLKFYNFD IHKAAFILPS FARSMIES
