PAO2_ARATH
ID PAO2_ARATH Reviewed; 490 AA.
AC Q9SKX5; Q8S9L4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Polyamine oxidase 2 {ECO:0000303|PubMed:21081665};
DE Short=AtPAO2 {ECO:0000303|PubMed:21081665};
DE EC=1.5.3.- {ECO:0000269|PubMed:21081665};
DE AltName: Full=Amine oxidase 1 {ECO:0000303|Ref.1};
GN Name=PAO2 {ECO:0000303|PubMed:21081665};
GN OrderedLocusNames=At2g43020 {ECO:0000312|Araport:AT2G43020};
GN ORFNames=MFL8.12 {ECO:0000312|EMBL:AAD22129.1};
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 [MRNA].
RA Pinontoan R., Cunningham K.W., Iida H., Uozumi N., Muto S.;
RT "A putative amine oxidase 1 from Arabidopsis.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP INDUCTION.
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 [9]
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, 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).
RN [11]
RP FUNCTION.
RX PubMed=26310141; DOI=10.1016/j.plaphy.2015.08.003;
RA Wimalasekera R., Schaarschmidt F., Angelini R., Cona A., Tavladoraki P.,
RA Scherer G.F.;
RT "POLYAMINE OXIDASE2 of Arabidopsis contributes to ABA mediated plant
RT developmental processes.";
RL Plant Physiol. Biochem. 96:231-240(2015).
CC -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion
CC (PubMed:20532512, PubMed:21081665). Catalyzes the oxidation of the
CC secondary amino group of polyamines, such as spermine, spermidine and
CC their acetyl derivatives (PubMed:20532512, PubMed:21081665). Substrate
CC preference is N(1)-acetylspermine > spermine > spermidine
CC (PubMed:21081665). Plays an important role in the regulation of
CC polyamine intracellular concentration (Probable). Involved in abscisic
CC acid-mediated developmental processes (PubMed:26310141). May contribute
CC to nitric oxide-mediated effects on root growth (PubMed:26310141).
CC {ECO:0000269|PubMed:20532512, ECO:0000269|PubMed:21081665,
CC ECO:0000269|PubMed:26310141, ECO:0000305|PubMed:21081665}.
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; Evidence={ECO:0000269|PubMed:21081665};
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;
CC Evidence={ECO:0000269|PubMed:21081665};
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; Evidence={ECO:0000269|PubMed:21081665};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:21081665};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:21081665};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.27 mM for spermine {ECO:0000269|PubMed:21081665};
CC KM=0.409 mM for spermidine {ECO:0000269|PubMed:21081665};
CC KM=0.233 mM for N(1)-acetylspermine {ECO:0000269|PubMed:21081665};
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:18703589}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers and siliques. Also
CC found in leaf and stem and in low levels in cotyledons, roots and in
CC seedlings.
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; AF364952; AAO85404.1; -; mRNA.
DR EMBL; AC006224; AAD22129.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10199.1; -; Genomic_DNA.
DR EMBL; AY074846; AAL75899.1; -; mRNA.
DR EMBL; BT029025; ABI93934.1; -; mRNA.
DR PIR; A84861; A84861.
DR RefSeq; NP_181830.1; NM_129863.3.
DR AlphaFoldDB; Q9SKX5; -.
DR SMR; Q9SKX5; -.
DR BioGRID; 4241; 1.
DR STRING; 3702.AT2G43020.1; -.
DR PaxDb; Q9SKX5; -.
DR PRIDE; Q9SKX5; -.
DR ProteomicsDB; 236831; -.
DR EnsemblPlants; AT2G43020.1; AT2G43020.1; AT2G43020.
DR GeneID; 818904; -.
DR Gramene; AT2G43020.1; AT2G43020.1; AT2G43020.
DR KEGG; ath:AT2G43020; -.
DR Araport; AT2G43020; -.
DR TAIR; locus:2053723; AT2G43020.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_10_0_1; -.
DR InParanoid; Q9SKX5; -.
DR OMA; EFFDNYQ; -.
DR OrthoDB; 1034142at2759; -.
DR PhylomeDB; Q9SKX5; -.
DR BioCyc; ARA:AT2G43020-MON; -.
DR BRENDA; 1.5.3.17; 399.
DR UniPathway; UPA00211; -.
DR UniPathway; UPA00250; -.
DR PRO; PR:Q9SKX5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKX5; baseline and differential.
DR Genevisible; Q9SKX5; AT.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0052903; F:N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:RHEA.
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:RHEA.
DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:RHEA.
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..490
FT /note="Polyamine oxidase 2"
FT /id="PRO_0000352508"
FT MOTIF 488..490
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 246
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 433
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT CONFLICT 288
FT /note="E -> G (in Ref. 4; AAL75899)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 54321 MW; 48E8EBD38AEC1E8E CRC64;
MESRKNSDRQ MRRANCFSAG ERMKTRSPSV IVIGGGFGGI SAARTLQDAS FQVMVLESRD
RIGGRVHTDY SFGFPVDLGA SWLHGVCKEN PLAPVIGRLG LPLYRTSGDN SVLYDHDLES
YALFDMDGNQ VPQELVTQIG VTFERILEEI NKVRDEQDAD ISISQAFSIV FSRKPELRLE
GLAHNVLQWY VCRMEGWFAA DAETISAKCW DQEELLPGGH GLMVRGYRPV INTLAKGLDI
RVGHRVTKIV RRYNGVKVTT ENGQTFVADA AVIAVPLGVL KSGTIKFEPK LPEWKQEAIN
DLGVGIENKI ILHFEKVFWP KVEFLGVVAE TSYGCSYFLN LHKATGHPVL VYMPAGQLAK
DIEKMSDEAA ANFAVLQLQR ILPDALPPVQ YLVSRWGSDV NSMGSYSYDI VGKPHDLYER
LRVPVDNLFF AGEATSSSFP GSVHGAYSTG LMAAEDCRMR VLERYGELDL FQPVMGEEGP
ASVPLLISRL
