PMT1_TOBAC
ID PMT1_TOBAC Reviewed; 375 AA.
AC Q42963; A0A1S3Y3K4; Q9SEH6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Putrescine N-methyltransferase 1 {ECO:0000303|PubMed:10598105};
DE Short=NtPMT1a {ECO:0000303|PubMed:10598105};
DE EC=2.1.1.53 {ECO:0000255|PROSITE-ProRule:PRU00947, ECO:0000269|PubMed:8038607, ECO:0000269|PubMed:9620262};
DE AltName: Full=A411 {ECO:0000303|PubMed:8038607};
GN Name=PMT1 {ECO:0000303|PubMed:10598105};
GN ORFNames=LOC107771646 {ECO:0000312|RefSeq:XP_016446557.1};
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, PATHWAY, TISSUE SPECIFICITY, REPRESSION BY AUXIN, AND INDUCTION
RP BY YOUNG AERIAL TISSUES REMOVAL.
RC STRAIN=cv. Burley 21; TISSUE=Root;
RX PubMed=8038607; DOI=10.2307/3869875;
RA Hibi N., Higashiguchi S., Hashimoto T., Yamada Y.;
RT "Gene expression in tobacco low-nicotine mutants.";
RL Plant Cell 6:723-735(1994).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9620262; DOI=10.1023/a:1005961122814;
RA Hashimoto T., Shoji T., Mihara T., Oguri H., Tamaki K., Suzuki K.,
RA Yamada Y.;
RT "Intraspecific variability of the tandem repeats in Nicotiana putrescine N-
RT methyltransferases.";
RL Plant Mol. Biol. 37:25-37(1998).
RN [5]
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 [6]
RP INDUCTION BY JASMONATE.
RC STRAIN=cv. Burley 21;
RX PubMed=10965939; DOI=10.1093/pcp/pcd001;
RA Shoji T., Yamada Y., Hashimoto T.;
RT "Jasmonate induction of putrescine N-methyltransferase genes in the root of
RT Nicotiana sylvestris.";
RL Plant Cell Physiol. 41:831-839(2000).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. NC95;
RX PubMed=14756309; DOI=10.1023/b:plan.0000009268.45851.95;
RA Chintapakorn Y., Hamill J.D.;
RT "Antisense-mediated down-regulation of putrescine N-methyltransferase
RT activity in transgenic Nicotiana tabacum L. can lead to elevated levels of
RT anatabine at the expense of nicotine.";
RL Plant Mol. Biol. 53:87-105(2003).
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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:8038607, PubMed:31276744,
CC PubMed:34095742). Methyltransferase that mediates the conversion of
CC putrescine to N-methylputrescine (PubMed:8038607, PubMed:9620262).
CC Promotes leaves ripening (PubMed:34095742).
CC {ECO:0000269|PubMed:31276744, ECO:0000269|PubMed:34095742,
CC ECO:0000269|PubMed:8038607, ECO:0000269|PubMed:9620262}.
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 ECO:0000269|PubMed:8038607, ECO:0000269|PubMed:9620262};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000269|PubMed:8038607}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots.
CC {ECO:0000269|PubMed:10598105, ECO:0000269|PubMed:8038607}.
CC -!- INDUCTION: Down-regulated by auxin (PubMed:8038607). Accumulates upon
CC the removal of flower heads and young leaves (PubMed:8038607,
CC PubMed:10598105). Triggered by jasmonic acid (MeJA) (PubMed:10965939,
CC PubMed:15604714, PubMed:9869416). {ECO:0000269|PubMed:10598105,
CC ECO:0000269|PubMed:10965939, ECO:0000269|PubMed:15604714,
CC ECO:0000269|PubMed:8038607, ECO:0000269|PubMed:9869416}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of anatabine at the expense of
CC nicotine (PubMed:14756309). Plants suppressed for PMT1, PMT2, PMT3 and
CC PMT4 exhibit strongly reduced nicotine levels but accumulate polyamines
CC in roots, and have an impaired leaf maturation phenotype at harvest
CC (PubMed:34095742). {ECO:0000269|PubMed:14756309,
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D28506; BAA05867.1; -; mRNA.
DR EMBL; AF126810; AAF14879.1; -; Genomic_DNA.
DR PIR; T03681; T03681.
DR RefSeq; NP_001312037.1; NM_001325108.1.
DR RefSeq; XP_016446557.1; XM_016591071.1.
DR AlphaFoldDB; Q42963; -.
DR SMR; Q42963; -.
DR STRING; 4097.Q42963; -.
DR GeneID; 107771646; -.
DR KEGG; nta:107771646; -.
DR OrthoDB; 1059849at2759; -.
DR BRENDA; 2.1.1.53; 3645.
DR UniPathway; UPA00107; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0030750; F:putrescine N-methyltransferase activity; IDA:UniProtKB.
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:0009733; P:response to auxin; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alkaloid metabolism; Methyltransferase; Polyamine biosynthesis;
KW Putrescine biosynthesis; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..375
FT /note="Putrescine N-methyltransferase 1"
FT /id="PRO_0000156541"
FT DOMAIN 86..323
FT /note="PABS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00354"
FT REGION 24..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00354,
FT ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 192
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 223..224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 311
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT CONFLICT 308
FT /note="V -> A (in Ref. 1; BAA05867)"
SQ SEQUENCE 375 AA; 41142 MW; 856483D2DB270D88 CRC64;
MEVISTNTNG STIFKNGAIP MNGHQNGTSE HLNGYQNGTS KHQNGHQNGT FEHRNGHQNG
TSEQQNGTIS HDNGNELLGS SDSIKPGWFS EFSALWPGEA FSLKVEKLLF QGKSDYQDVM
LFESATYGKV LTLDGAIQHT ENGGFPYTEM IVHLPLGSIP NPKKVLIIGG GIGFTLFEML
RYPSIEKIDI VEIDDVVVDV SRKFFPYLAA NFNDPRVTLV LGDGAAFVKA AQAGYYDAII
VDSSDPIGPA KDLFERPFFE AVAKALRPGG VVCTQAESIW LHMHIIKQII ANCRQVFKGS
VNYAWTTVPT YPTGVIGYML CSTEGPEVDF KNPVNPIDKE TTQVKSKLGP LKFYNSDIHK
AAFILPSFAR SMIES
