NAMT1_ARATH
ID NAMT1_ARATH Reviewed; 359 AA.
AC Q9SCP7; A0A178VFV7;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Nicotinate N-methyltransferase 1 {ECO:0000303|PubMed:28533213};
DE Short=AtNANMT1 {ECO:0000303|PubMed:28533213};
DE EC=2.1.1.7 {ECO:0000269|PubMed:28533213};
GN Name=NANMT1 {ECO:0000303|PubMed:28533213};
GN OrderedLocusNames=At3g53140 {ECO:0000312|Araport:AT3G53140};
GN ORFNames=T4D2.70 {ECO:0000312|EMBL:CAB64217.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASN-21; TYR-120; HIS-124
RP AND THR-264.
RX PubMed=28533213; DOI=10.1104/pp.17.00259;
RA Li W., Zhang F., Wu R., Jia L., Li G., Guo Y., Liu C., Wang G.;
RT "A novel N-methyltransferase in Arabidopsis appears to feed a conserved
RT pathway for nicotinate detoxification among land plants and is associated
RT with lignin biosynthesis.";
RL Plant Physiol. 174:1492-1504(2017).
CC -!- FUNCTION: Involved in nicotinate detoxification in planta
CC (PubMed:28533213). Catalyzes the conversion of nicotinate to N-
CC methylnicotinate, which is a detoxified form of endogenous nicotinate
CC in planta (PubMed:28533213). {ECO:0000269|PubMed:28533213}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=nicotinate + S-adenosyl-L-methionine = N-methylnicotinate + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:20241, ChEBI:CHEBI:18123,
CC ChEBI:CHEBI:32544, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.7;
CC Evidence={ECO:0000269|PubMed:28533213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20242;
CC Evidence={ECO:0000269|PubMed:28533213};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38.7 uM for nicotinate {ECO:0000269|PubMed:28533213};
CC KM=52.13 uM for S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:28533213};
CC Note=kcat is 3.52 sec(-1) with nicotinate as substrate
CC (PubMed:28533213). kcat is 3.01 sec(-1) with S-adenosyl-L-methionine
CC as substrate (PubMed:28533213). {ECO:0000269|PubMed:28533213};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28533213}.
CC -!- TISSUE SPECIFICITY: Highly expressed in anthers, pistils, developing
CC siliques, and developing seeds. {ECO:0000269|PubMed:28533213}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AL132958; CAB64217.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79041.1; -; Genomic_DNA.
DR EMBL; AF367289; AAK56277.1; -; mRNA.
DR EMBL; AY133618; AAM91448.1; -; mRNA.
DR PIR; T46160; T46160.
DR RefSeq; NP_190882.1; NM_115174.2.
DR AlphaFoldDB; Q9SCP7; -.
DR SMR; Q9SCP7; -.
DR STRING; 3702.AT3G53140.1; -.
DR PaxDb; Q9SCP7; -.
DR PRIDE; Q9SCP7; -.
DR ProMEX; Q9SCP7; -.
DR ProteomicsDB; 189785; -.
DR EnsemblPlants; AT3G53140.1; AT3G53140.1; AT3G53140.
DR GeneID; 824480; -.
DR Gramene; AT3G53140.1; AT3G53140.1; AT3G53140.
DR KEGG; ath:AT3G53140; -.
DR Araport; AT3G53140; -.
DR TAIR; locus:2102038; AT3G53140.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_12_1_1; -.
DR InParanoid; Q9SCP7; -.
DR OMA; IYIDYFY; -.
DR OrthoDB; 817726at2759; -.
DR PhylomeDB; Q9SCP7; -.
DR BioCyc; ARA:AT3G53140-MON; -.
DR BRENDA; 2.1.1.7; 399.
DR Proteomes; UP000006548; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0008168; F:methyltransferase activity; IDA:TAIR.
DR GO; GO:0008938; F:nicotinate N-methyltransferase activity; IDA:TAIR.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR GO; GO:1901847; P:nicotinate metabolic process; IDA:TAIR.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF08100; Dimerisation; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..359
FT /note="Nicotinate N-methyltransferase 1"
FT /id="PRO_0000451460"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT MUTAGEN 21
FT /note="N->S: Reduces catalytic activity 4-fold."
FT /evidence="ECO:0000269|PubMed:28533213"
FT MUTAGEN 120
FT /note="Y->L: Reduces catalytic activity 2-fold."
FT /evidence="ECO:0000269|PubMed:28533213"
FT MUTAGEN 124
FT /note="H->N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28533213"
FT MUTAGEN 264
FT /note="T->H: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28533213"
SQ SEQUENCE 359 AA; 39688 MW; 5847B43BF7563781 CRC64;
MENESSESRN RARLAIMELA NMISVPMSLN AAVRLGIADA IWNGGANSPL SAAEILPRLH
LPSHTTIGGD PENLQRILRM LTSYGVFSEH LVGSIERKYS LTDVGKTLVT DSGGLSYAAY
VLQHHQEALM RAWPLVHTAV VEPETEPYVK ANGEAAYAQY GKSEEMNGLM QKAMSGVSVP
FMKAILDGYD GFKSVDILVD VGGSAGDCLR MILQQFPNVR EGINFDLPEV VAKAPNIPGV
THVGGDMFQS VPSADAIFMK WVLTTWTDEE CKQIMKNCYN ALPVGGKLIA CEPVLPKETD
ESHRTRALLE GDIFVMTIYR TKGKHRTEEE FIELGLSAGF PTFRPFYIDY FYTILEFQK
