PMT4_TOBAC
ID PMT4_TOBAC Reviewed; 386 AA.
AC Q9SEH4; A0A1S3XYW1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Putrescine N-methyltransferase 4 {ECO:0000303|PubMed:10598105};
DE Short=NtPMT4 {ECO:0000303|PubMed:10598105};
DE EC=2.1.1.53 {ECO:0000255|PROSITE-ProRule:PRU00947};
GN Name=PMT4 {ECO:0000303|PubMed:10598105};
GN ORFNames=LOC107770255 {ECO:0000312|RefSeq:XP_016445029.1};
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 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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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; AF126812; AAF14881.1; -; Genomic_DNA.
DR RefSeq; XP_016445029.1; XM_016589543.1.
DR AlphaFoldDB; Q9SEH4; -.
DR SMR; Q9SEH4; -.
DR STRING; 4097.Q9SEH4; -.
DR GeneID; 107770255; -.
DR KEGG; nta:107770255; -.
DR OMA; TNHENGN; -.
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; 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; 2.
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..386
FT /note="Putrescine N-methyltransferase 4"
FT /id="PRO_0000156544"
FT DOMAIN 97..334
FT /note="PABS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00354"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00354,
FT ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 234..235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT BINDING 322
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00947"
FT CONFLICT 61
FT /note="I -> ISEHQNGHQNGTSEHRNGHQNGISEHQNGHQNGT (in Ref. 1;
FT AAF14881)"
SQ SEQUENCE 386 AA; 42289 MW; B42339E403BB49A9 CRC64;
MEVISTNTNG STIFKNGAIP MNGHQSGTSK HLNGYQNGTS KHQNGHHNGT SEHRNGHQNG
ISEHQNGHQN GTSEQQNGTI SHDNGNELLG NSNSIKLGWF SEFSALWPGE AFSLKVEKLL
FQGKSDYQDV MLFESATYGK VLTLDGAIQH TENGGFPYTE MIVHLPLGSI PNPKKVLIIG
GGIGFTLFEM LRYPTIEKID IVEIDDVVVD VSRKSFPYLA ANFNDPRVTL VLGDGAAFVK
AAQAGYYDAI IVDSSDPIGP AKDLFERPFF EAVAKALRPG GVVCTQAESI WLHMHIIKQI
IANCRQVFKG SVNYAWTTVP TYPTGVIGYM LCSTEGPEVD FKNPINPIDK ETTQVKSKLA
PLKFYNSDIH KAAFILPSFA RSMIES
