DAO1_TOBAC
ID DAO1_TOBAC Reviewed; 786 AA.
AC A0A1S3XSG2;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Diamine oxidase [copper-containing] 1, peroxisomal {ECO:0000303|PubMed:24287136};
DE Short=NtDAO1 {ECO:0000303|PubMed:24287136};
DE EC=1.4.3.- {ECO:0000269|PubMed:24287136};
DE AltName: Full=Copper methylamine oxidase;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P46883};
DE AltName: Full=N-methylputrescine oxidase 2, peroxisomal {ECO:0000303|PubMed:17283012};
DE Short=NtMPO2 {ECO:0000303|PubMed:17283012};
DE EC=1.4.3.- {ECO:0000250|UniProtKB:A0A1S4BDC4};
GN Name=DAO1 {ECO:0000303|PubMed:24287136};
GN Synonyms=MPO2 {ECO:0000303|PubMed:17283012};
GN ORFNames=LOC107768026 {ECO:0000312|RefSeq:XP_016442617.1};
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 [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 [2]
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 [3]
RP TISSUE SPECIFICITY.
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, PATHWAY, AND TISSUE SPECIFICITY.
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 [6]
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 putrescine catabolism in peroxisomes
CC (PubMed:24287136). May also be involved in the biosynthesis of pyridine
CC alkaloid natural products, leading mainly to the production of
CC anabasine, anatabine, nicotine and nornicotine, effective deterrents
CC against herbivores with antiparasitic and pesticide properties
CC (neurotoxins); nornicotine serves as the precursor in the synthesis of
CC the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:16656744).
CC Oxidizes preferentially non-N-methylated amines (PubMed:24287136).
CC {ECO:0000269|PubMed:16656744, 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:24287136};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154;
CC Evidence={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:0000250|UniProtKB:A0A1S4BDC4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71016;
CC Evidence={ECO:0000250|UniProtKB:A0A1S4BDC4};
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=163 uM for putrescine {ECO:0000269|PubMed:24287136};
CC KM=478 uM for N-methylputrescine {ECO:0000269|PubMed:24287136};
CC KM=492 uM for cadaverine {ECO:0000269|PubMed:24287136};
CC Vmax=561 pmol/sec/mg enzyme with putrescine as substrate
CC {ECO:0000269|PubMed:24287136};
CC Vmax=928 pmol/sec/mg enzyme with N-methylputrescine as substrate
CC {ECO:0000269|PubMed:24287136};
CC Vmax=840 pmol/sec/mg enzyme with cadaverine as substrate
CC {ECO:0000269|PubMed:24287136};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000269|PubMed:16656744}.
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation.
CC {ECO:0000269|PubMed:24287136}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A1S4BDC4}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24287136}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots, and, to a lower extent,
CC in leaves and stems. {ECO:0000269|PubMed:17283012,
CC 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 -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR RefSeq; XP_016442617.1; XM_016587131.1.
DR SMR; A0A1S3XSG2; -.
DR GeneID; 107768026; -.
DR KEGG; nta:107768026; -.
DR OMA; EMCNESK; -.
DR OrthoDB; 1320015at2759; -.
DR UniPathway; UPA00107; -.
DR UniPathway; UPA00188; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
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: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:0050232; F:putrescine oxidase 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 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..786
FT /note="Diamine oxidase [copper-containing] 1, peroxisomal"
FT /id="PRO_0000455787"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 505
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 419..430
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 502..507
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 555
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 557
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 710
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 711
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 721
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT SITE 784..786
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 505
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT DISULFID 440..466
FT /evidence="ECO:0000250|UniProtKB:P12807"
SQ SEQUENCE 786 AA; 87421 MW; BFC0C7041AEB39DF CRC64;
MATTKQKVTA PSSSTAPCCP STSILRREAT AAVAGVGDGL QNWNNVPSVD DKQKKTASSA
LASLASTEPL SSNTSTKGIQ IMTRAQTCHP LDPLSAAEIS VAVATVRAAG ETPEVRDGMR
FIEVVLLEPD KSVVALADAY FFPPFQSSLM PRTKGGSLIP TKLPPRRARL IVYNKKTNET
SIWIVELNEV HAAARGGHHR GKVISSNVVP DVQPPIDAQE YAECEAVVKS YPPFRDAMRR
RGIDDLDLVM VDPWCVGYHS EADAPSRRLA KPLVFCRTES DCPMENGYAR PVEGIYVLVD
VQNMQIIEFE DRKLVPLPPA DPLRNYTAGE TRGGVDRSDV KPLHIIQPEG PSFRISGNYI
EWQKWNFRIG FTPREGLVIH SVAYLDGSRG RRPIAHRLSF VEMVVPYGDP NDPHYRKNAF
DAGEDGLGKN AHSLKRGCDC LGYIKYFDAH FTNFTGGVET TENCVCLHEE DHGMLWKHQD
WRTGLAEVRR SRRLTVSFVC TVANYEYAFY WHFYQDGKIE AEVKLTGILS LGALQPGEYR
KYGTTILPGL YAPVHQHFFV ARMNMAVDCK PGEAHNQVVE VNVKVEEPGK ENVHNNAFYA
EETLLRSELQ AMRDCDPFSA RHWIVRNTRT VNRTGQLTGY KLVPGPNCLP LAGPEAKFLR
RAAFLKHNLW VTQYAPGEEF PGGEFPNQNP RVGEGLASWV KQDRPLEESD IVLWYIFGIT
HVPRLEDWPV MPVEHIGFVL QPHGFFNCSP AVDVPPPSAC DSESRDSDVT ETSVAKSTAT
SLLAKL
