PMT3_NICAT
ID PMT3_NICAT Reviewed; 388 AA.
AC A0A314LG79;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Putrescine N-methyltransferase 3 {ECO:0000303|Ref.1};
DE EC=2.1.1.53 {ECO:0000255|PROSITE-ProRule:PRU00947};
GN Name=PMT3 {ECO:0000303|Ref.1};
GN ORFNames=A4A49_61142 {ECO:0000312|EMBL:OIT40668.1};
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 [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 [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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Spermidine/spermine synthase 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; MJEQ01000009; OIT40668.1; -; Genomic_DNA.
DR RefSeq; XP_019258255.1; XM_019402710.1.
DR EnsemblPlants; OIT40668; OIT40668; A4A49_61142.
DR GeneID; 109236516; -.
DR Gramene; OIT40668; OIT40668; A4A49_61142.
DR KEGG; nau:109236516; -.
DR UniPathway; UPA00107; -.
DR Proteomes; UP000187609; Unassembled WGS sequence.
DR GO; GO:0030750; F:putrescine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
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..388
FT /note="Putrescine N-methyltransferase 3"
FT /id="PRO_0000455798"
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; 42567 MW; 413E8C0C440A2925 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
LAPLKFYNSD IHKAAFILPS FARSMIES
