MPO1_TOBAC
ID MPO1_TOBAC Reviewed; 790 AA.
AC A0A1S4BDC4; A4GZ88;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=N-methylputrescine oxidase 1, peroxisomal {ECO:0000303|PubMed:17174363, ECO:0000303|PubMed:17283012};
DE Short=NtMPO1 {ECO:0000303|PubMed:17174363, ECO:0000303|PubMed:17283012};
DE EC=1.4.3.- {ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136};
DE AltName: Full=Copper methylamine oxidase;
DE EC=1.4.3.21 {ECO:0000269|PubMed:24287136};
GN Name=MPO1 {ECO:0000303|PubMed:17174363, ECO:0000303|PubMed:17283012};
GN ORFNames=LOC107807126 {ECO:0000312|RefSeq:XP_016486930.1};
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, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, INDUCTION BY AUXIN AND JASMONATE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Burley 21; TISSUE=Root;
RX PubMed=17174363; DOI=10.1016/j.phytochem.2006.11.003;
RA Heim W.G., Sykes K.A., Hildreth S.B., Sun J., Lu R.-H., Jelesko J.G.;
RT "Cloning and characterization of a Nicotiana tabacum methylputrescine
RT oxidase transcript.";
RL Phytochemistry 68:454-463(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY,
RP INDUCTION BY JASMONATE, AND SUBUNIT.
RX PubMed=17283012; DOI=10.1093/pcp/pcm018;
RA Katoh A., Shoji T., Hashimoto T.;
RT "Molecular cloning of N-methylputrescine oxidase from tobacco.";
RL Plant Cell Physiol. 48:550-554(2007).
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 PATHWAY.
RX PubMed=16656744; DOI=10.1104/pp.43.1.93;
RA Mizusaki S., Kisaki T., Tamaki E.;
RT "Phytochemical Studies on the Tobacco Alkaloids. XII. Identification of
RT gamma-Methylaminobutyraldehyde and its Precursor Role in Nicotine
RT Biosynthesis.";
RL Plant Physiol. 43:93-98(1968).
RN [5]
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 [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY JASMONIC ACID.
RX PubMed=24287136; DOI=10.1093/pcp/pct179;
RA Naconsie M., Kato K., Shoji T., Hashimoto T.;
RT "Molecular evolution of N-methylputrescine oxidase in tobacco.";
RL Plant Cell Physiol. 55:436-444(2014).
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).
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:17174363, PubMed:17283012,
CC PubMed:16656744). Amine oxidase which mediates the deamination of N-
CC methylputrescine to produce 4-methylaminobutanal (PubMed:17174363,
CC PubMed:17283012). Oxidizes preferentially N-methylated amines
CC (PubMed:24287136). {ECO:0000269|PubMed:16656744,
CC ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012,
CC ECO:0000269|PubMed:24287136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012,
CC ECO:0000269|PubMed:24287136};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154;
CC Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012,
CC ECO:0000269|PubMed:24287136};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-methylputrescine + O2 = 4-methylaminobutanal + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:71015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58039,
CC ChEBI:CHEBI:190141; Evidence={ECO:0000269|PubMed:17174363,
CC ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71016;
CC Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012,
CC ECO:0000269|PubMed:24287136};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P12807};
CC Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc
CC ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807,
CC ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000250|UniProtKB:P46883};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=309 uM for putrescine {ECO:0000269|PubMed:24287136};
CC KM=57 uM for N-methylputrescine {ECO:0000269|PubMed:24287136};
CC KM=215 uM for cadaverine {ECO:0000269|PubMed:24287136};
CC KM=0.19 mM for N-methylputrescine {ECO:0000269|PubMed:17174363};
CC KM=0.76 mM for putrescine {ECO:0000269|PubMed:17174363};
CC KM=1.79 mM for cadaverine {ECO:0000269|PubMed:17174363};
CC KM=0.35 mM for 1,3-diaminopropane {ECO:0000269|PubMed:17174363};
CC KM=36 uM for N-methylputrescine {ECO:0000269|PubMed:17283012};
CC KM=247 uM for putrescine {ECO:0000269|PubMed:17283012};
CC KM=362 uM for cadaverine {ECO:0000269|PubMed:17283012};
CC KM=158 uM for 1,3-diaminopropane {ECO:0000269|PubMed:17283012};
CC KM=96 uM for N-methyl-1,3-diaminopropane
CC {ECO:0000269|PubMed:17283012};
CC KM=249 uM for n-butylamine {ECO:0000269|PubMed:17283012};
CC Vmax=28.8 nmol/sec/mg enzyme with N-methylputrescine as substrate
CC {ECO:0000269|PubMed:17174363};
CC Vmax=11.1 nmol/sec/mg enzyme with putrescine as substrate
CC {ECO:0000269|PubMed:17174363};
CC Vmax=5.2 nmol/sec/mg enzyme with cadaverine as substrate
CC {ECO:0000269|PubMed:17174363};
CC Vmax=11.3 nmol/sec/mg enzyme with 1,3-diaminopropane as substrate
CC {ECO:0000269|PubMed:17174363};
CC Vmax=926 pmol/sec/mg enzyme with N-methylputrescine as substrate
CC {ECO:0000269|PubMed:17283012};
CC Vmax=902 pmol/sec/mg enzyme with putrescine as substrate
CC {ECO:0000269|PubMed:17283012};
CC Vmax=715 pmol/sec/mg enzyme with cadaverine as substrate
CC {ECO:0000269|PubMed:17283012};
CC Vmax=666 pmol/sec/mg enzyme with 1,3-diaminopropane as substrate
CC {ECO:0000269|PubMed:17283012};
CC Vmax=1270 pmol/sec/mg enzyme with N-methyl-1,3-diaminopropane as
CC substrate {ECO:0000269|PubMed:17283012};
CC Vmax=862 pmol/sec/mg enzyme with n-butylamine as substrate
CC {ECO:0000269|PubMed:17283012};
CC Vmax=750 pmol/sec/mg enzyme with putrescine as substrate
CC {ECO:0000269|PubMed:24287136};
CC Vmax=512 pmol/sec/mg enzyme with N-methylputrescine as substrate
CC {ECO:0000269|PubMed:24287136};
CC Vmax=920 pmol/sec/mg enzyme with cadaverine as substrate
CC {ECO:0000269|PubMed:24287136};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000269|PubMed:16656744, ECO:0000269|PubMed:17174363,
CC ECO:0000269|PubMed:17283012}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17283012}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24287136}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots, and, to a lower extent,
CC in stems. {ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012,
CC ECO:0000269|PubMed:24287136}.
CC -!- INDUCTION: Accumulates in roots upon auxin deprivation
CC (PubMed:17174363). Induced by jasmonic acid (MeJA) (PubMed:17174363,
CC PubMed:17283012, PubMed:24287136). {ECO:0000269|PubMed:17174363,
CC ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
CC -!- DISRUPTION PHENOTYPE: Altered nicotine biosynthesis.
CC {ECO:0000269|PubMed:17283012}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR EMBL; DQ873385; ABI93948.1; -; mRNA.
DR EMBL; AB289456; BAF49519.1; -; mRNA.
DR RefSeq; NP_001312728.1; NM_001325799.1.
DR RefSeq; XP_016486930.1; XM_016631444.1.
DR SMR; A0A1S4BDC4; -.
DR GeneID; 107807126; -.
DR KEGG; nta:107807126; -.
DR OMA; VAYDECD; -.
DR OrthoDB; 1320015at2759; -.
DR BioCyc; MetaCyc:MON-12442; -.
DR SABIO-RK; A0A1S4BDC4; -.
DR UniPathway; UPA00107; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0052599; F:methylputrescine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0042179; P:nicotine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Copper; Disulfide bond; Manganese; Metal-binding;
KW Oxidoreductase; Peroxisome; Reference proteome; TPQ.
FT CHAIN 1..790
FT /note="N-methylputrescine oxidase 1, peroxisomal"
FT /id="PRO_0000455786"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 509
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 423..434
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 506..511
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 559
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 561
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 714
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 715
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 725
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT SITE 788..790
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 509
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT DISULFID 444..470
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CONFLICT 309
FT /note="Q -> K (in Ref. 1; ABI93948 and 2; BAF49519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 87966 MW; B1582D36B15E9903 CRC64;
MATTKQKVTA PSPSPSSSTA SCCPSTSILR REATAAIAVV GDGLQNWTNI PSVDEKQKKT
ASSALASLPT TEPLSTNTST KGIQIMTRAQ TCHPLDPLSA AEISVAVATV RAAGETPEVR
DGMRFIEVVL VEPDKSVVAL ADAYFFPPFQ SSLMPRTKGG SQIPTKLPPR RARLIVYNKK
TNETSIWIVE LNEVHAAARG GHHRGKVIAS NVVPDVQPPI DAQEYAECEA VVKSYPPFRD
AMRRRGIDDL DLVMVDPWCV GYHSEADAPS RRLAKPLVFC RTESDCPMEN GYARPVEGIY
VLVDVQNMQI IEFEDRKLVP LPPVDPLRNY TAGETRGGVD RSDVKPLHII QPEGPSFRIS
GNYVEWQKWN FRIGFTPREG LVIHSVAYLD GSRGRRPIAH RLSFVEMVVP YGDPNDPHYR
KNAFDAGEDG LGKNAHSLKR GCDCLGYIKY FDAHFTNFTG GVETTENCVC LHEEDHGMLW
KHQDWRTGLA EVRRSRRLTV SFVCTVANYE YAFYWHFYQD GKIEAEVKLT GILSLGALQP
GEYRKYGTTI LPGLYAPVHQ HFFVARMNMA VDCKPGEAHN QVVEVNVKVE EPGKENVHNN
AFYAEETLLR SELQAMRDCD PFSARHWIVR NTRTVNRTGQ LTGYKLVPGP NCLPLAGPEA
KFLRRAAFLK HNLWVTQYAP GEDFPGGEFP NQNPRVGEGL ASWVKQDRPL EESDIVLWYI
FGITHVPRLE DWPVMPVEHI GFVLQPHGYF NCSPAVDVPP PFACDSESRD SDVTETSVAK
STATSLLAKL
