ID PAO5_ARATH Reviewed; 533 AA.
AC Q9SU79;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=Probable polyamine oxidase 5 {ECO:0000303|PubMed:16778015};
DE Short=AtPAO5 {ECO:0000303|PubMed:16778015};
DE EC=1.5.3.- {ECO:0000269|PubMed:24550437};
GN Name=PAO5 {ECO:0000303|PubMed:16778015};
GN OrderedLocusNames=At4g29720 {ECO:0000312|Araport:AT4G29720};
GN ORFNames=T16L4.230 {ECO:0000312|EMBL:CAB45332.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
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].
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 [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 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=24550437; DOI=10.1093/jxb/eru016;
RA Ahou A., Martignago D., Alabdallah O., Tavazza R., Stano P., Macone A.,
RA Pivato M., Masi A., Rambla J.L., Vera-Sirera F., Angelini R., Federico R.,
RA Tavladoraki P.;
RT "A plant spermine oxidase/dehydrogenase regulated by the proteasome and
RT polyamines.";
RL J. Exp. Bot. 65:1585-1603(2014).
RN [9]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24906355; DOI=10.1104/pp.114.242610;
RA Kim D.W., Watanabe K., Murayama C., Izawa S., Niitsu M., Michael A.J.,
RA Berberich T., Kusano T.;
RT "Polyamine oxidase5 regulates Arabidopsis growth through thermospermine
RT oxidase activity.";
RL Plant Physiol. 165:1575-1590(2014).
RN [10]
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).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28199662; DOI=10.1093/jxb/erw510;
RA Alabdallah O., Ahou A., Mancuso N., Pompili V., Macone A., Pashkoulov D.,
RA Stano P., Cona A., Angelini R., Tavladoraki P.;
RT "The Arabidopsis polyamine oxidase/dehydrogenase 5 interferes with
RT cytokinin and auxin signaling pathways to control xylem differentiation.";
RL J. Exp. Bot. 68:997-1012(2017).
CC -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion
CC (PubMed:24550437, PubMed:24906355, PubMed:26973665, PubMed:28199662).
CC Catalyzes the oxidation of the secondary amino group of polyamines,
CC such as spermine and its acetyl derivatives (PubMed:24550437,
CC PubMed:24906355, PubMed:28199662). Substrate preference is spermine >
CC N(1)-acetylspermine > thermospermine > norspermine (PubMed:24550437).
CC Plays an important role in the regulation of polyamine intracellular
CC concentration (PubMed:24550437, PubMed:26973665, PubMed:28199662).
CC Involved in xylem differentiation by controlling thermospermine
CC homeostasis, and participating in the tightly controlled interplay
CC between auxin and cytokinin that is necessary for proper xylem
CC differentiation (PubMed:28199662). Involved in the production of
CC hydrogen peroxide in response to salt and cold stresses
CC (PubMed:26973665). {ECO:0000269|PubMed:24550437,
CC ECO:0000269|PubMed:24906355, ECO:0000269|PubMed:26973665,
CC ECO:0000269|PubMed:28199662}.
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:24550437};
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:24550437};
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;
CC Evidence={ECO:0000269|PubMed:24550437};
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:24550437};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:24550437};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:24550437};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.18 uM for N(1)-acetylspermine (at pH 6.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24906355};
CC KM=1.92 uM for N(1)-acetylspermine (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24906355};
CC KM=13.65 uM for thermospermine (at pH 6.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24906355};
CC KM=5.09 uM for thermospermine (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24906355};
CC KM=15.81 uM for norspermine (at pH 6.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24906355};
CC KM=25.54 uM for norspermine (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24906355};
CC KM=78.67 uM for spermine (at pH 6.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24906355};
CC KM=25.56 uM for spermine (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24906355};
CC pH dependence:
CC Optimum pH is 6.5 with thermospermine as substrate (PubMed:24906355).
CC Optimum pH is 7.5 with spermine as substrate (PubMed:24906355).
CC {ECO:0000269|PubMed:24906355};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius with thermospermine as
CC substrate (PubMed:24906355). Optimum temperature is 35-45 degrees
CC Celsius with spermine as substrate (PubMed:24906355).
CC {ECO:0000269|PubMed:24906355};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24550437,
CC ECO:0000269|PubMed:24906355, ECO:0000305|PubMed:26973665}.
CC -!- TISSUE SPECIFICITY: Expressed in root vasculature, leaves and stems.
CC {ECO:0000269|PubMed:26973665}.
CC -!- INDUCTION: Induced by salicylic acid (PubMed:18583528). Down-regulated
CC upon treatment with flagellin 22, a pathogen elicitor
CC (PubMed:18583528). Induced by auxin, cytokinin and thermospermine in
CC roots (PubMed:28199662). Induced by spermine, thermospermine, N-
CC acetylspermine and spermidine in roots (PubMed:24550437).
CC {ECO:0000269|PubMed:18583528, ECO:0000269|PubMed:24550437,
CC ECO:0000269|PubMed:28199662}.
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). Increased length and thickness of floral stems
CC (PubMed:28199662). Increased length of roots (PubMed:28199662). Delayed
CC transition from vegetative to reproductive stage (PubMed:24906355).
CC Increased levels of thermospermine (PubMed:24906355).
CC {ECO:0000269|PubMed:24906355, ECO:0000269|PubMed:26973665,
CC ECO:0000269|PubMed:28199662}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AL079344; CAB45332.1; -; Genomic_DNA.
DR EMBL; AL161575; CAB79730.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85665.1; -; Genomic_DNA.
DR EMBL; AK118203; BAC42825.1; -; mRNA.
DR EMBL; BT005501; AAO63921.1; -; mRNA.
DR EMBL; AY085576; AAM62798.1; -; mRNA.
DR PIR; T09935; T09935.
DR RefSeq; NP_194701.1; NM_119117.2.
DR AlphaFoldDB; Q9SU79; -.
DR SMR; Q9SU79; -.
DR STRING; 3702.Q9SU79; -.
DR iPTMnet; Q9SU79; -.
DR PaxDb; 3702-AT4G29720-1; -.
DR ProteomicsDB; 236832; -.
DR EnsemblPlants; AT4G29720.1; AT4G29720.1; AT4G29720.
DR GeneID; 829093; -.
DR Gramene; AT4G29720.1; AT4G29720.1; AT4G29720.
DR KEGG; ath:AT4G29720; -.
DR Araport; AT4G29720; -.
DR TAIR; AT4G29720; PAO5.
DR eggNOG; KOG0685; Eukaryota.
DR HOGENOM; CLU_004498_2_3_1; -.
DR InParanoid; Q9SU79; -.
DR OMA; EIMLLWE; -.
DR OrthoDB; 2642916at2759; -.
DR PhylomeDB; Q9SU79; -.
DR BRENDA; 1.5.3.13; 399.
DR BRENDA; 1.5.3.16; 399.
DR BRENDA; 1.5.3.17; 399.
DR UniPathway; UPA00211; -.
DR PRO; PR:Q9SU79; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU79; baseline and differential.
DR Genevisible; Q9SU79; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:EnsemblPlants.
DR GO; GO:0052903; F:N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:EnsemblPlants.
DR GO; GO:0052894; F:norspermine:oxygen oxidoreductase activity; IEA:EnsemblPlants.
DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:EnsemblPlants.
DR GO; GO:1990534; F:thermospermine oxidase activity; IMP:TAIR.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:TAIR.
DR GO; GO:0046208; P:spermine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1903602; P:thermospermine catabolic process; IEA:EnsemblPlants.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF405; PEROXISOMAL N(1)-ACETYL-SPERMINE_SPERMIDINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; Oxidoreductase; Reference proteome;
KW Stress response.
FT CHAIN 1..533
FT /note="Probable polyamine oxidase 5"
FT /id="PRO_0000352511"
FT BINDING 37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 262
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 501
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
SQ SEQUENCE 533 AA; 58686 MW; 789CBBF64F5624F3 CRC64;
MAKKARIVII GAGMAGLTAA NKLYTSSNNT FELSVVEGGS RIGGRINTSE FSSEKIEMGA
TWIHGIGGSP VYRIAKETGS LVSDEPWECM DSTIDKAKTF AEGGFEIEPS IVESISGLFT
ALMELAQGKE ISQSDADLSR LAHIYETATR VCSKGSSTSV GSFLKSGFDA YWDSISNGGE
EGVKGYGKWS RKSLEEAIFT MFSNTQRTYT SADELSTLDF AAESEYQMFP GEEITIAKGY
LSVIHHLASV LPQGVIQLNR KVTKIEWQSN EVKLHFSDGS VVFADHVIVT VSLGVLKAGI
ETDAELFSPP LPDFKSDAIR RLGYGVVNKL FVEMSQRKFP SLQLVFDRED SEFRFVKIPW
WMRRTATITP IHSNSKVLLS WFAGKEALEL EKLTDEEIKD AVMTTISCLT GKEVKNDTAK
PLTNGSLNDD DEAMKITKVL KSKWGSDPLF RGSYSYVAVG SSGDDLDAMA EPLPKINKKV
GQVNGHDQAK VHELQVMFAG EATHRTHYST THGAYYSGLR EANRLLKHYK CNF
//
