A0A1S4BDC4 · MPO1_TOBAC
- ProteinN-methylputrescine oxidase 1, peroxisomal
- GeneMPO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids790 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:16656744, PubMed:17174363, PubMed:17283012).
Amine oxidase which mediates the deamination of N-methylputrescine to produce 4-methylaminobutanal (PubMed:17174363, PubMed:17283012).
Oxidizes preferentially N-methylated amines (PubMed:24287136).
Amine oxidase which mediates the deamination of N-methylputrescine to produce 4-methylaminobutanal (PubMed:17174363, PubMed:17283012).
Oxidizes preferentially N-methylated amines (PubMed:24287136).
Catalytic activity
- a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4+This reaction proceeds in the forward direction.
- H2O + N-methylputrescine + O2 = 4-methylaminobutanal + H2O2 + NH4+This reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Binds 1 copper ion per subunit (By similarity).
Can also use zinc ion as cofactor (By similarity).
Can also use zinc ion as cofactor (By similarity).
Note: Contains 1 topaquinone per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
309 μM | putrescine | |||||
57 μM | N-methylputrescine | |||||
215 μM | cadaverine | |||||
0.19 mM | N-methylputrescine | |||||
0.76 mM | putrescine | |||||
1.79 mM | cadaverine | |||||
0.35 mM | 1,3-diaminopropane | |||||
36 μM | N-methylputrescine | |||||
247 μM | putrescine | |||||
362 μM | cadaverine | |||||
158 μM | 1,3-diaminopropane | |||||
96 μM | N-methyl-1,3-diaminopropane | |||||
249 μM | n-butylamine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
28.8 nmol/sec/mg | with N-methylputrescine as substrate | ||||
11.1 nmol/sec/mg | with putrescine as substrate | ||||
5.2 nmol/sec/mg | with cadaverine as substrate | ||||
11.3 nmol/sec/mg | with 1,3-diaminopropane as substrate | ||||
926 pmol/sec/mg | with N-methylputrescine as substrate | ||||
902 pmol/sec/mg | with putrescine as substrate | ||||
715 pmol/sec/mg | with cadaverine as substrate | ||||
666 pmol/sec/mg | with 1,3-diaminopropane as substrate | ||||
1270 pmol/sec/mg | with N-methyl-1,3-diaminopropane as substrate | ||||
862 pmol/sec/mg | with n-butylamine as substrate | ||||
750 pmol/sec/mg | with putrescine as substrate | ||||
512 pmol/sec/mg | with N-methylputrescine as substrate | ||||
920 pmol/sec/mg | with cadaverine as substrate |
Pathway
Alkaloid biosynthesis; nicotine biosynthesis.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 423-434 | substrate | ||||
Sequence: AFDAGEDGLGKN | ||||||
Active site | 425 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 506-511 | substrate | ||||
Sequence: VANYEY | ||||||
Active site | 509 | Schiff-base intermediate with substrate; via topaquinone | ||||
Sequence: Y | ||||||
Binding site | 559 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 561 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 714 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 715 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 725 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 788-790 | Microbody targeting signal | ||||
Sequence: AKL |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisome | |
Molecular Function | aliphatic amine oxidase activity | |
Molecular Function | copper ion binding | |
Molecular Function | identical protein binding | |
Molecular Function | methylputrescine oxidase activity | |
Molecular Function | primary amine oxidase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | quinone binding | |
Biological Process | alkaloid metabolic process | |
Biological Process | amine metabolic process | |
Biological Process | nicotine biosynthetic process | |
Biological Process | response to auxin | |
Biological Process | response to jasmonic acid |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-methylputrescine oxidase 1, peroxisomal
- EC number
- Short namesNtMPO1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Solanales > Solanaceae > Nicotianoideae > Nicotianeae > Nicotiana
Accessions
- Primary accessionA0A1S4BDC4
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Altered nicotine biosynthesis.
PTM/Processing
Features
Showing features for chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000455786 | 1-790 | N-methylputrescine oxidase 1, peroxisomal | |||
Sequence: MATTKQKVTAPSPSPSSSTASCCPSTSILRREATAAIAVVGDGLQNWTNIPSVDEKQKKTASSALASLPTTEPLSTNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLVEPDKSVVALADAYFFPPFQSSLMPRTKGGSQIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVIASNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVPLPPVDPLRNYTAGETRGGVDRSDVKPLHIIQPEGPSFRISGNYVEWQKWNFRIGFTPREGLVIHSVAYLDGSRGRRPIAHRLSFVEMVVPYGDPNDPHYRKNAFDAGEDGLGKNAHSLKRGCDCLGYIKYFDAHFTNFTGGVETTENCVCLHEEDHGMLWKHQDWRTGLAEVRRSRRLTVSFVCTVANYEYAFYWHFYQDGKIEAEVKLTGILSLGALQPGEYRKYGTTILPGLYAPVHQHFFVARMNMAVDCKPGEAHNQVVEVNVKVEEPGKENVHNNAFYAEETLLRSELQAMRDCDPFSARHWIVRNTRTVNRTGQLTGYKLVPGPNCLPLAGPEAKFLRRAAFLKHNLWVTQYAPGEDFPGGEFPNQNPRVGEGLASWVKQDRPLEESDIVLWYIFGITHVPRLEDWPVMPVEHIGFVLQPHGYFNCSPAVDVPPPFACDSESRDSDVTETSVAKSTATSLLAKL | ||||||
Disulfide bond | 444↔470 | |||||
Sequence: CLGYIKYFDAHFTNFTGGVETTENCVC | ||||||
Modified residue | 509 | 2',4',5'-topaquinone | ||||
Sequence: Y |
Post-translational modification
Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Keywords
- PTM
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length790
- Mass (Da)87,966
- Last updated2017-04-12 v1
- ChecksumB1582D36B15E9903
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A9B4SPQ8 | A0A9B4SPQ8_TOBAC | LOC107807126 | 790 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 309 | in Ref. 1; ABI93948 and 2; BAF49519 | ||||
Sequence: Q → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ873385 EMBL· GenBank· DDBJ | ABI93948.1 EMBL· GenBank· DDBJ | mRNA | ||
AB289456 EMBL· GenBank· DDBJ | BAF49519.1 EMBL· GenBank· DDBJ | mRNA |