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PMT3_TOBAC
ID   PMT3_TOBAC              Reviewed;         381 AA.
AC   Q9SEH5; A0A1S4ANJ0; I1Z0D3; L7SV57;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Putrescine N-methyltransferase 3 {ECO:0000303|PubMed:10598105};
DE            Short=NtPMT3 {ECO:0000303|PubMed:10598105};
DE            EC=2.1.1.53 {ECO:0000255|PROSITE-ProRule:PRU00947};
GN   Name=PMT3 {ECO:0000303|PubMed:10598105};
GN   ORFNames=LOC107799425 {ECO:0000312|RefSeq:XP_016478023.1};
OS   Nicotiana tabacum (Common 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=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION BY YOUNG
RP   AERIAL TISSUES REMOVAL, AND GENE FAMILY.
RC   STRAIN=cv. Xanthi;
RX   PubMed=10598105; DOI=10.1023/a:1006342018991;
RA   Riechers D.E., Timko M.P.;
RT   "Structure and expression of the gene family encoding putrescine N-
RT   methyltransferase in Nicotiana tabacum: new clues to the evolutionary
RT   origin of cultivated tobacco.";
RL   Plant Mol. Biol. 41:387-401(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90;
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-375.
RC   STRAIN=cv. Sindoro-1;
RA   Basuki S., Mattjik N.A.A., Suwarso X., Wirnas D., Sudarsono S.;
RT   "Isolation of genes encoding putrescine N-methyltransferase and quinolinat
RT   phosphoribosyl transferase derived from Temanggung tobacco cultivar
RT   (Nicotiana tabacum).";
RL   J. Penelit. Tanam. Ind. 17:109-117(2011).
RN   [4]
RP   INDUCTION BY JASMONATE.
RC   STRAIN=cv. Bright Yellow 2;
RX   PubMed=9869416; DOI=10.1023/a:1006058700949;
RA   Imanishi S., Hashizume K., Nakakita M., Kojima H., Matsubayashi Y.,
RA   Hashimoto T., Sakagami Y., Yamada Y., Nakamura K.;
RT   "Differential induction by methyl jasmonate of genes encoding ornithine
RT   decarboxylase and other enzymes involved in nicotine biosynthesis in
RT   tobacco cell cultures.";
RL   Plant Mol. Biol. 38:1101-1111(1998).
RN   [5]
RP   INDUCTION BY JASMONATE.
RC   STRAIN=cv. Bright Yellow 2;
RX   PubMed=15604714; DOI=10.1007/s11103-004-1962-8;
RA   Xu B., Timko M.;
RT   "Methyl jasmonate induced expression of the tobacco putrescine N
RT   -methyltransferase genes requires both G-box and GCC-motif elements.";
RL   Plant Mol. Biol. 55:743-761(2004).
RN   [6]
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   [7]
RP   REVIEW ON ALKALOID BIOSYNTHESIS IN NICOTIANA TABACUM.
RX   PubMed=23953973; DOI=10.1016/j.phytochem.2013.06.002;
RA   Dewey R.E., Xie J.;
RT   "Molecular genetics of alkaloid biosynthesis in Nicotiana tabacum.";
RL   Phytochemistry 94:10-27(2013).
RN   [8]
RP   REVIEW ON NICOTINE BIOSYNTHESIS.
RX   PubMed=25582664; DOI=10.1007/s00438-015-0989-7;
RA   Wang X., Bennetzen J.L.;
RT   "Current status and prospects for the study of Nicotiana genomics,
RT   genetics, and nicotine biosynthesis genes.";
RL   Mol. Genet. Genomics 290:11-21(2015).
RN   [9]
RP   FUNCTION.
RC   STRAIN=cv. Burley Stella, cv. Burley TN90, cv. Virginia ITB 683, and
RC   cv. Virginia K326;
RX   PubMed=31276744; DOI=10.1016/j.fct.2019.110660;
RA   Schorderet Weber S., Kaminski K.P., Perret J.-L., Leroy P., Mazurov A.,
RA   Peitsch M.C., Ivanov N.V., Hoeng J.;
RT   "Antiparasitic properties of leaf extracts derived from selected Nicotiana
RT   species and Nicotiana tabacum varieties.";
RL   Food Chem. Toxicol. 132:110660-110660(2019).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Burley TN90 LC;
RX   PubMed=34095742; DOI=10.1002/pld3.329;
RA   Noelke G., Chudobova I., Houdelet M., Volke D., Lusso M., Frederick J.,
RA   Kudithipudi C., Shen Y., Warek U., Strickland J.A., Xu D., Schinkel H.,
RA   Schillberg S.;
RT   "Impact of nicotine pathway downregulation on polyamine biosynthesis and
RT   leaf ripening in tobacco.";
RL   Plant Direct 5:e00329-e00329(2021).
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) (PubMed:10598105, PubMed:31276744,
CC       PubMed:34095742). Methyltransferase that mediates the conversion of
CC       putrescine to N-methylputrescine (PubMed:10598105). Promotes leaves
CC       ripening (PubMed:34095742). {ECO:0000269|PubMed:31276744,
CC       ECO:0000269|PubMed:34095742, ECO:0000303|PubMed:10598105}.
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. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in roots.
CC       {ECO:0000269|PubMed:10598105}.
CC   -!- INDUCTION: Accumulates upon the removal of flower heads and young
CC       leaves (PubMed:10598105). Triggered by jasmonic acid (MeJA)
CC       (PubMed:15604714, PubMed:9869416). {ECO:0000269|PubMed:10598105,
CC       ECO:0000269|PubMed:15604714, ECO:0000269|PubMed:9869416}.
CC   -!- DISRUPTION PHENOTYPE: Plants suppressed for PMT1, PMT2, PMT3 and PMT4
CC       exhibit strongly reduced nicotine levels but accumulate polyamines in
CC       roots, and have an impaired leaf maturation phenotype at harvest.
CC       {ECO:0000269|PubMed:34095742}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Putrescine methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00947}.
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DR   EMBL; AF126811; AAF14880.1; -; Genomic_DNA.
DR   EMBL; JQ438825; AFJ11561.1; -; Genomic_DNA.
DR   EMBL; JX978277; AGC24706.1; -; mRNA.
DR   RefSeq; XP_016478023.1; XM_016622537.1.
DR   AlphaFoldDB; Q9SEH5; -.
DR   SMR; Q9SEH5; -.
DR   STRING; 4097.Q9SEH5; -.
DR   GeneID; 107799425; -.
DR   KEGG; nta:107799425; -.
DR   OrthoDB; 1059849at2759; -.
DR   PhylomeDB; Q9SEH5; -.
DR   BRENDA; 2.1.1.53; 3645.
DR   UniPathway; UPA00107; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0030750; F:putrescine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004766; F:spermidine synthase activity; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0042179; P:nicotine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009753; P:response to jasmonic acid; 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   Putrescine biosynthesis; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..381
FT                   /note="Putrescine N-methyltransferase 3"
FT                   /id="PRO_0000156543"
FT   DOMAIN          92..329
FT                   /note="PABS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00354"
FT   REGION          21..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        248
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00354,
FT                   ECO:0000255|PROSITE-ProRule:PRU00947"
FT   BINDING         123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT   BINDING         198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT   BINDING         229..230
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT   BINDING         317
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT   CONFLICT        107
FT                   /note="F -> S (in Ref. 3; AGC24706)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        238
FT                   /note="Q -> H (in Ref. 3; AFJ11561)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351
FT                   /note="K -> E (in Ref. 3; AFJ11561)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  41795 MW;  A19DE2B83CE4D530 CRC64;
     MEVISTNTNG STIFKNGAIP MNGYQNGTSK HQNGHQNGTS EHRNGHQNGI SEHQNGHQNG
     TSEHQNGHQN GTISHDNGNE LQLLGSSNSI KPGWFSEFSA LWPGEAFSLK VEKLLFQGKS
     DYQDVMLFES ATYGKVLTLD GAIQHTENGG FPYTEMIVHL PLGSIPNPKK VLIIGGGIGF
     TLFEMLRYPT IEKIDIVEID DVVVDVSRKF FPYLAANFSD PRVTLVLGDG AAFVKAAQAG
     YYDAIIVDSS DPIGPAKDLF ERPFFEAVAK ALRPGGVVCT QAESIWLHMH IIKQIIANCR
     QVFKGSVNYA WTTVPTYPTG VIGYMLCSTE GPEVDFKNPV NPIDKETTQV KSKLAPLKFY
     NSDIHKAAFI LPSFARSMIE S
 
 
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