PMT2_NICAT
ID PMT2_NICAT Reviewed; 371 AA.
AC Q93XQ4; A0A314LHN6;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Putrescine N-methyltransferase 2 {ECO:0000303|PubMed:11299398};
DE Short=NaPMT2 {ECO:0000303|PubMed:11299398};
DE EC=2.1.1.53 {ECO:0000255|PROSITE-ProRule:PRU00947};
GN Name=PMT2 {ECO:0000303|PubMed:11299398};
GN ORFNames=A4A49_05615 {ECO:0000312|EMBL:OIT40667.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UT; TISSUE=Leaf;
RA Xu S., Brockmoeller T., Gaquerel E., Navarro 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., Baldwin I.T.;
RT "The genome of Nicotiana attenuata.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=OIT40667.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF280403; AAK49871.1; -; mRNA.
DR EMBL; MJEQ01000009; OIT40667.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_019258257.1; XM_019402712.1.
DR RefSeq; XP_019258258.1; XM_019402713.1.
DR EnsemblPlants; OIT40667; OIT40667; A4A49_05615.
DR GeneID; 109236517; -.
DR Gramene; OIT40667; OIT40667; A4A49_05615.
DR KEGG; nau:109236517; -.
DR OrthoDB; 1059849at2759; -.
DR BRENDA; 2.1.1.53; 9729.
DR UniPathway; UPA00107; -.
DR Proteomes; UP000187609; Unassembled WGS sequence.
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 Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..371
FT /note="Putrescine N-methyltransferase 2"
FT /id="PRO_0000455797"
FT DOMAIN 82..319
FT /note="PABS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00354"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00354,
FT ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 219..220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 307
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
SQ SEQUENCE 371 AA; 40698 MW; DC6149417C19C08F CRC64;
MEVISTNTNG STIFKNGAIP MNGHQNGTSK HQNGTSEHPN GHQNGTSEHQ NGHQNGTSEQ
QNGTISHDNG NKLVGNSNCI KPGWFSEFSA LWPGEAFSLK VEKLLFQGKS DYQDVMLFES
ATYGKVLTLD GAIQHTENGG FPYTEMIVHL PLGSIPNPKK VLIIGGGIGF TLFEMLRYPS
IEKIDIVEID DVVVDVSRKF FPYLAANFND PRVTLVLGDG AAFVKAAQAE YYDAIIVDSS
DPIGPAKDLF ERPFFEAVAK ALRPGGVVCT QAESIWLHMH IIKQIIANCR QVFKGSVNYA
WTTVPTYPTG VIGYMLCSTE GPEVDFKNPV NPIDKETTQV KPKLAPLKFY NSDIHKAAFI
LPSFARSMIE S
