PAO3_ARATH
ID PAO3_ARATH Reviewed; 488 AA.
AC Q9LYT1; Q8LE44;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Polyamine oxidase 3 {ECO:0000303|PubMed:18583528};
DE Short=AtPAO3 {ECO:0000303|PubMed:18583528};
DE EC=1.5.3.17 {ECO:0000269|PubMed:18583528};
GN Name=PAO3 {ECO:0000303|PubMed:18583528};
GN OrderedLocusNames=At3g59050 {ECO:0000312|Araport:AT3G59050};
GN ORFNames=F17J16.100 {ECO:0000312|EMBL:CAB86933.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=16778015; DOI=10.1104/pp.106.080911;
RA Tavladoraki P., Rossi M.N., Saccuti G., Perez-Amador M.A., Polticelli F.,
RA Angelini R., Federico R.;
RT "Heterologous expression and biochemical characterization of a polyamine
RT oxidase from Arabidopsis involved in polyamine back conversion.";
RL Plant Physiol. 141:1519-1532(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18703589; DOI=10.1093/pcp/pcn114;
RA Kamada-Nobusada T., Hayashi M., Fukazawa M., Sakakibara H., Nishimura M.;
RT "A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine
RT catabolism in Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:1272-1282(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18583528; DOI=10.1104/pp.108.123802;
RA Moschou P.N., Sanmartin M., Andriopoulou A.H., Rojo E.,
RA Sanchez-Serrano J.J., Roubelakis-Angelakis K.A.;
RT "Bridging the gap between plant and mammalian polyamine catabolism: a novel
RT peroxisomal polyamine oxidase responsible for a full back-conversion
RT pathway in Arabidopsis thaliana.";
RL Plant Physiol. 147:1845-1857(2008).
RN [8]
RP FUNCTION.
RX PubMed=20532512; DOI=10.1007/s00299-010-0881-1;
RA Takahashi Y., Cong R., Sagor G.H., Niitsu M., Berberich T., Kusano T.;
RT "Characterization of five polyamine oxidase isoforms in Arabidopsis
RT thaliana.";
RL Plant Cell Rep. 29:955-965(2010).
RN [9]
RP FUNCTION.
RX PubMed=20626657; DOI=10.1111/j.1365-313x.2010.04301.x;
RA Wu J., Shang Z., Wu J., Jiang X., Moschou P.N., Sun W.,
RA Roubelakis-Angelakis K.A., Zhang S.;
RT "Spermidine oxidase-derived H(2)O(2) regulates pollen plasma membrane
RT hyperpolarization-activated Ca(2+) -permeable channels and pollen tube
RT growth.";
RL Plant J. 63:1042-1053(2010).
RN [10]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21081665; DOI=10.1093/jxb/erq341;
RA Fincato P., Moschou P.N., Spedaletti V., Tavazza R., Angelini R.,
RA Federico R., Roubelakis-Angelakis K.A., Tavladoraki P.;
RT "Functional diversity inside the Arabidopsis polyamine oxidase gene
RT family.";
RL J. Exp. Bot. 62:1155-1168(2011).
CC -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion
CC (PubMed:18583528, PubMed:20532512, PubMed:21081665). Catalyzes the
CC oxidation of the secondary amino group of polyamines, such as spermine,
CC spermidine and their acetyl derivatives (PubMed:18583528,
CC PubMed:20532512, PubMed:21081665). Substrate preference is spermidine >
CC spermine > N(1)-acetylspermidine > N(1)-acetylspermine
CC (PubMed:18583528). Plays an important role in the regulation of
CC polyamine intracellular concentration (Probable). Involved in the
CC production of hydrogen peroxide during pollen tube growth
CC (PubMed:20626657). Hydrogen peroxide triggers the opening of the
CC hyperpolarization-activated calcium permeable channels in pollen, and
CC thus regulates pollen tube growth (PubMed:20626657).
CC {ECO:0000269|PubMed:18583528, ECO:0000269|PubMed:20532512,
CC ECO:0000269|PubMed:20626657, ECO:0000269|PubMed:21081665,
CC ECO:0000305|PubMed:18583528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + spermine = 3-aminopropanal + H2O2 + spermidine;
CC Xref=Rhea:RHEA:25804, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:45725, ChEBI:CHEBI:57834,
CC ChEBI:CHEBI:58374; EC=1.5.3.17;
CC Evidence={ECO:0000269|PubMed:18583528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + spermidine = 3-aminopropanal + H2O2 + putrescine;
CC Xref=Rhea:RHEA:25808, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:57834, ChEBI:CHEBI:58374,
CC ChEBI:CHEBI:326268; EC=1.5.3.17;
CC Evidence={ECO:0000269|PubMed:18583528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermine + O2 = 3-acetamidopropanal + H2O2 +
CC spermidine; Xref=Rhea:RHEA:25800, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:58101; EC=1.5.3.17;
CC Evidence={ECO:0000269|PubMed:18583528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermidine + O2 = 3-acetamidopropanal + H2O2
CC + putrescine; Xref=Rhea:RHEA:25812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:58324, ChEBI:CHEBI:326268; EC=1.5.3.17;
CC Evidence={ECO:0000269|PubMed:18583528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + thermospermine = 3-aminopropanal + H2O2 +
CC spermidine; Xref=Rhea:RHEA:57836, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57834,
CC ChEBI:CHEBI:58374, ChEBI:CHEBI:59903;
CC Evidence={ECO:0000269|PubMed:18583528};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by guazatine, aminoguanidine and
CC putrescine. {ECO:0000269|PubMed:18583528}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.204 mM for spermidine {ECO:0000269|PubMed:18583528};
CC KM=0.274 mM for spermidine {ECO:0000269|PubMed:21081665};
CC KM=0.588 mM for spermine {ECO:0000269|PubMed:18583528};
CC KM=0.58 mM for spermine {ECO:0000269|PubMed:21081665};
CC KM=1 mM for N(1)-acetylspermidine {ECO:0000269|PubMed:18583528};
CC KM=2 mM for N(1)-acetylspermine {ECO:0000269|PubMed:18583528,
CC ECO:0000269|PubMed:21081665};
CC KM=0.045 mM for norspermine {ECO:0000269|PubMed:21081665};
CC KM=0.05 mM for thermospermine {ECO:0000269|PubMed:21081665};
CC pH dependence:
CC Optimum pH is 7.5. No activity at pH above 9.5 or below 6.5.
CC {ECO:0000269|PubMed:18583528};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:18583528};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305}.
CC -!- PATHWAY: Amine and polyamine degradation; spermidine degradation.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:18583528,
CC ECO:0000269|PubMed:18703589}.
CC -!- TISSUE SPECIFICITY: Expressed at similar levels in all tissues tested.
CC Highest expression is seen in siliques. {ECO:0000269|PubMed:18583528}.
CC -!- INDUCTION: By abscisic acid, jasmonate, salicylic acid, wounding and
CC flagellin 22, a pathogen elicitor. {ECO:0000269|PubMed:18583528}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AL163527; CAB86933.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79866.1; -; Genomic_DNA.
DR EMBL; AY065025; AAL57665.1; -; mRNA.
DR EMBL; AY143905; AAN28844.1; -; mRNA.
DR EMBL; AY085634; AAM62855.1; -; mRNA.
DR PIR; T47787; T47787.
DR RefSeq; NP_191464.1; NM_115767.3.
DR AlphaFoldDB; Q9LYT1; -.
DR SMR; Q9LYT1; -.
DR BioGRID; 10389; 7.
DR IntAct; Q9LYT1; 1.
DR STRING; 3702.AT3G59050.1; -.
DR PaxDb; Q9LYT1; -.
DR PRIDE; Q9LYT1; -.
DR ProteomicsDB; 236268; -.
DR EnsemblPlants; AT3G59050.1; AT3G59050.1; AT3G59050.
DR GeneID; 825074; -.
DR Gramene; AT3G59050.1; AT3G59050.1; AT3G59050.
DR KEGG; ath:AT3G59050; -.
DR Araport; AT3G59050; -.
DR TAIR; locus:2077670; AT3G59050.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_10_0_1; -.
DR InParanoid; Q9LYT1; -.
DR OMA; WCKRIEC; -.
DR OrthoDB; 1034142at2759; -.
DR PhylomeDB; Q9LYT1; -.
DR BioCyc; ARA:AT3G59050-MON; -.
DR BioCyc; MetaCyc:AT3G59050-MON; -.
DR BRENDA; 1.5.3.17; 399.
DR UniPathway; UPA00211; -.
DR UniPathway; UPA00250; -.
DR PRO; PR:Q9LYT1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYT1; baseline and differential.
DR Genevisible; Q9LYT1; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0052904; F:N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052903; F:N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase activity; IDA:TAIR.
DR GO; GO:0052902; F:spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0006598; P:polyamine catabolic process; IDA:TAIR.
DR GO; GO:0046203; P:spermidine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046208; P:spermine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..488
FT /note="Polyamine oxidase 3"
FT /id="PRO_0000352509"
FT MOTIF 486..488
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 434
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT CONFLICT 247
FT /note="I -> V (in Ref. 4; AAM62855)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="K -> N (in Ref. 4; AAM62855)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="L -> M (in Ref. 4; AAM62855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 54132 MW; 1EC37D18794A2BD4 CRC64;
MESGGKTNRQ LRKAICVSTD EKMKKKRSPS VIVIGGGMAG ISAARTLQDA SFQVVVLESR
DRIGGRVHTD YSFGFPVDLG ASWLHGVCKE NPLAAVIGRL GLPLYRTSGD NSVLYDHDLE
SYALFDKAGN QVSQELVTKV GENFEHILEE ICKVRDEQDE DMSIAQAFSI VFKRNPELRL
EGLAHNVLQW YLCRMEGWFA ADAETISAKC WDQEELLPGG HGLMVRGYRP VINTLSKGLD
IRLSHRITKI SRRYSGVKVT TEKGDTFVAD AAVIALPLGV LKSGMITFEP KLPQWKQEAI
NDLGVGIENK IILNFDNVFW PNVEFLGVVA ETSYGCSYFL NLHKATSHPV LVYMPAGQLA
RDIEKKSDEA AANFAFSQLQ KILPDASSPI NYLVSRWGSD INSLGSYSYD IVNKPHDLYE
RLRVPLDNLF FAGEATSSSY PGSVHGAYST GVLAAEDCRM RVLERYGELE HEMEEEAPAS
VPLLISRM
