PAO1_ARATH
ID PAO1_ARATH Reviewed; 472 AA.
AC Q9FNA2; Q7FL79;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Polyamine oxidase 1 {ECO:0000303|PubMed:16778015};
DE Short=AtPAO1 {ECO:0000303|PubMed:16778015};
DE EC=1.5.3.16 {ECO:0000269|PubMed:16778015};
DE EC=1.5.3.17 {ECO:0000269|PubMed:16778015};
DE AltName: Full=N(1)-acetylpolyamine oxidase {ECO:0000305};
DE AltName: Full=Spermine oxidase {ECO:0000305};
GN Name=PAO1 {ECO:0000303|PubMed:16778015};
GN Synonyms=PAO {ECO:0000303|PubMed:11432750};
GN OrderedLocusNames=At5g13700 {ECO:0000312|Araport:AT5G13700};
GN ORFNames=MSH12.17 {ECO:0000312|EMBL:BAB08697.1};
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=11432750; DOI=10.1046/j.1432-1327.2001.02296.x;
RA Cervelli M., Cona A., Angelini R., Polticelli F., Federico R.,
RA Mariottini P.;
RT "A barley polyamine oxidase isoform with distinct structural features and
RT subcellular localization.";
RL Eur. J. Biochem. 268:3816-3830(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
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 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 [8]
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).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26973665; DOI=10.3389/fpls.2016.00214;
RA Sagor G.H., Zhang S., Kojima S., Simm S., Berberich T., Kusano T.;
RT "Reducing cytoplasmic polyamine oxidase activity in Arabidopsis increases
RT salt and drought tolerance by reducing reactive oxygen species production
RT and increasing defense gene expression.";
RL Front. Plant Sci. 7:214-214(2016).
CC -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion
CC (PubMed:16778015, PubMed:20532512, PubMed:21081665, PubMed:26973665).
CC Catalyzes the oxidation of the secondary amino group of polyamines,
CC such as spermine and its acetyl derivatives (PubMed:16778015,
CC PubMed:20532512, PubMed:21081665). Substrate preference is
CC thermospermine > norspermine > spermine > N(1)-acetylspermine
CC (PubMed:16778015, PubMed:21081665). No activity detected when
CC putrescine, spermidine or N(1)-acetylspermidine are used as substrates
CC (PubMed:16778015). Plays an important role in the regulation of
CC polyamine intracellular concentration (Probable) (PubMed:26973665).
CC Involved in the production of hydrogen peroxide in response to salt and
CC cold stresses (PubMed:26973665). {ECO:0000269|PubMed:16778015,
CC ECO:0000269|PubMed:20532512, ECO:0000269|PubMed:21081665,
CC ECO:0000269|PubMed:26973665, ECO:0000305|PubMed:16778015}.
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=1.5.3.16;
CC Evidence={ECO:0000269|PubMed:16778015};
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:16778015};
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:16778015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + norspermine + O2 = 3-aminopropanal + H2O2 +
CC norspermidine; Xref=Rhea:RHEA:25816, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57920,
CC ChEBI:CHEBI:58374, ChEBI:CHEBI:58704; EC=1.5.3.16;
CC Evidence={ECO:0000269|PubMed:16778015};
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:16778015};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16778015};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:16778015};
CC -!- ACTIVITY REGULATION: Inhibited by guazatine, N-prenylagmatine and 1,12-
CC diaminododecane. {ECO:0000269|PubMed:16778015}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for spermine {ECO:0000269|PubMed:16778015};
CC KM=0.12 mM for spermine {ECO:0000269|PubMed:21081665};
CC KM=0.09 mM for norspermine {ECO:0000269|PubMed:16778015,
CC ECO:0000269|PubMed:21081665};
CC KM=0.2 mM for N(1)-acetylspermine {ECO:0000269|PubMed:16778015};
CC KM=0.47 mM for N(1)-acetylspermine {ECO:0000269|PubMed:21081665};
CC KM=0.02 mM for thermospermine {ECO:0000269|PubMed:21081665};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:16778015};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:26973665}.
CC -!- TISSUE SPECIFICITY: Expressed at very low levels in leaves, stems and
CC inflorescences. {ECO:0000269|PubMed:16778015}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype of seedlings under normal
CC growth conditions (PubMed:26973665). The double mutants pao1 and pao5
CC exhibit enhanced tolerance to salt and drought stress
CC (PubMed:26973665). {ECO:0000269|PubMed:26973665}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB006704; BAB08697.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91929.1; -; Genomic_DNA.
DR EMBL; AK118627; BAC43225.2; -; mRNA.
DR EMBL; BT026370; ABH04477.1; -; mRNA.
DR RefSeq; NP_196874.1; NM_121373.4.
DR AlphaFoldDB; Q9FNA2; -.
DR SMR; Q9FNA2; -.
DR BioGRID; 16493; 1.
DR STRING; 3702.AT5G13700.1; -.
DR PaxDb; Q9FNA2; -.
DR PRIDE; Q9FNA2; -.
DR EnsemblPlants; AT5G13700.1; AT5G13700.1; AT5G13700.
DR GeneID; 831215; -.
DR Gramene; AT5G13700.1; AT5G13700.1; AT5G13700.
DR KEGG; ath:AT5G13700; -.
DR Araport; AT5G13700; -.
DR TAIR; locus:2173219; AT5G13700.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_6_1_1; -.
DR InParanoid; Q9FNA2; -.
DR OMA; EAQAVDW; -.
DR OrthoDB; 508351at2759; -.
DR PhylomeDB; Q9FNA2; -.
DR BioCyc; ARA:AT5G13700-MON; -.
DR BioCyc; MetaCyc:AT5G13700-MON; -.
DR BRENDA; 1.5.3.16; 399.
DR BRENDA; 1.5.3.17; 399.
DR UniPathway; UPA00211; -.
DR PRO; PR:Q9FNA2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNA2; baseline and differential.
DR Genevisible; Q9FNA2; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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:0052895; F:N1-acetylspermine:oxygen oxidoreductase (N1-acetylspermidine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052894; F:norspermine:oxygen oxidoreductase 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: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; 2.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; Oxidoreductase; Reference proteome;
KW Stress response.
FT CHAIN 1..472
FT /note="Polyamine oxidase 1"
FT /id="PRO_0000352507"
FT BINDING 34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 213
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 405
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT CONFLICT 21
FT /note="V -> I (in Ref. 3; BAC43225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52866 MW; 139925C472DA57C6 CRC64;
MSTASVIIIG AGISGISAAK VLVENGVEDV LILEATDRIG GRIHKQNFGD VPVELGAGWI
AGVGGKESNP VWELASRFNL RTCFSDYTNA RFNIYDRSGK IFPTGIASDS YKKAVDSAIL
KLKSLEAQCS GQVAEEAPSS PKTPIELAID FILHDFEMAE VEPISTYVDF GEREFLVADE
RGYECLLYKM AEEFLVTSHG NILDYRLKLN QVVREVQQSR NGVVVKTEDG SVYEANYVIV
SASIGVLQSD LLSFQPLLPR WKTEAIQKCD VMVYTKIFLK FPQCFWPCGP GQEFFIYAHE
QRGYFTFWQH MENAYPGSNI LVVTLTNEQS KRVEAQSDQE TMKEAMSVLR DMFGATIPYA
TDILVPRWWN NRFQRGSYSN YPMISDNQLL QNIKAPVGRI FFTGEHTSEK FSGYVHGGYL
AGIDTSKSLL EEMKQSLLLQ PLLAFTESLT LTHQKPNNSQ IYTNVKFISG TS
