Reviewed, UniProtKB/Swiss-Prot Q9LYT1 (PAO3_ARATH)

Names and origin

Protein names

Recommended name:
    Polyamine oxidase 3
      Short name=AtPAO3
    EC=1.5.3.17

Gene names

Name:	PAO3
Ordered Locus Names:	At3g59050
ORF Names:	F17J16.100

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Flavoenzyme that catalyzes the sequential oxidation of spermine to spermidine, and of spermidine to putrescine. Substrate preference is spermidine > spermine > N(1)-acetylspermidine > N(1)-acetylspermine. No activity detected when diamines (agmatine, cadaverine or putrescine) or N(8)-acetylspermidine are used as substrates. Ref.6
Catalytic activity	Spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2. Ref.6 Spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2. Ref.6 N(1)-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2. N(1)-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2. Ref.6
Cofactor	Binds 1 FAD per subunit.
Enzyme regulation	Inhibited by guazatine, aminoguanidine and putrescine. Ref.6
Pathway	Amine and polyamine degradation; spermine degradation.
Subcellular location	Peroxisome Ref.6 Ref.5.
Tissue specificity	Expressed at similar levels in all tissues tested. Highest expression is seen in siliques. Ref.6
Induction	By abscisic acid, jasmonate, salicylic acid, wounding and flagellin 22, a pathogen elicitor. Ref.6
Sequence similarities	Belongs to the flavin monoamine oxidase family.
Biophysicochemical properties	Kinetic parameters: KM=0.204 mM for spermidine KM=0.588 mM for spermine KM=1 mM for N(1)-acetylspermidine KM=2 mM for N(1)-acetylspermine pH dependence: Optimum pH is 7.5. No activity at pH above 9.5 or below 6.5. Temperature dependence: Optimum temperature is 37 degrees Celsius.

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW polyamine catabolic process Ref.6 Inferred from direct assay. Source: TAIR
Cellular component	peroxisome Ref.6 Inferred from direct assay. Source: TAIR
Molecular function	polyamine oxidase activity Ref.6 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 488	488	Polyamine oxidase 3		PRO_0000352509
Experimental info
	Sequence conflict	247	1	I → V in AAM62855. Ref.3
	Sequence conflict	366	1	K → N in AAM62855. Ref.3
	Sequence conflict	404	1	L → M in AAM62855. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9LYT1-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 1EC37D18794A2BD4	FASTA	488	54,132
	10 20 30 40 50 60 MESGGKTNRQ LRKAICVSTD EKMKKKRSPS VIVIGGGMAG ISAARTLQDA SFQVVVLESR 70 80 90 100 110 120 DRIGGRVHTD YSFGFPVDLG ASWLHGVCKE NPLAAVIGRL GLPLYRTSGD NSVLYDHDLE 130 140 150 160 170 180 SYALFDKAGN QVSQELVTKV GENFEHILEE ICKVRDEQDE DMSIAQAFSI VFKRNPELRL 190 200 210 220 230 240 EGLAHNVLQW YLCRMEGWFA ADAETISAKC WDQEELLPGG HGLMVRGYRP VINTLSKGLD 250 260 270 280 290 300 IRLSHRITKI SRRYSGVKVT TEKGDTFVAD AAVIALPLGV LKSGMITFEP KLPQWKQEAI 310 320 330 340 350 360 NDLGVGIENK IILNFDNVFW PNVEFLGVVA ETSYGCSYFL NLHKATSHPV LVYMPAGQLA 370 380 390 400 410 420 RDIEKKSDEA AANFAFSQLQ KILPDASSPI NYLVSRWGSD INSLGSYSYD IVNKPHDLYE 430 440 450 460 470 480 RLRVPLDNLF FAGEATSSSY PGSVHGAYST GVLAAEDCRM RVLERYGELE HEMEEEAPAS VPLLISRM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion." Tavladoraki P., Rossi M.N., Saccuti G., Perez-Amador M.A., Polticelli F., Angelini R., Federico R. Plant Physiol. 141:1519-1532(2006) [PubMed: 16778015] [Abstract] Cited for: IDENTIFICATION.
[5]	"A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine catabolism in Arabidopsis thaliana." Kamada-Nobusada T., Hayashi M., Fukazawa M., Sakakibara H., Nishimura M. Plant Cell Physiol. 49:1272-1282(2008) [PubMed: 18703589] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis thaliana." Moschou P.N., Sanmartin M., Andriopoulou A.H., Rojo E., Sanchez-Serrano J.J., Roubelakis-Angelakis K.A. Plant Physiol. 147:1845-1857(2008) [PubMed: 18583528] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL163527 Genomic DNA. Translation: CAB86933.1. AY065025 mRNA. Translation: AAL57665.1. AY143905 mRNA. Translation: AAN28844.1. AY085634 mRNA. Translation: AAM62855.1.
IPI	IPI00545156.
PIR	T47787.
RefSeq	NP_191464.1.
UniGene	At.27590 Rra.13503 Rsa.18473
3D structure databases
HSSP	HSSP built from PDB template 1RSG based on UniProtKB P50264.
ModBase	Search...
Proteomic databases
PRIDE	Q9LYT1.
Genome annotation databases
GeneID	825074.
GenomeReviews	Gene locus AT3G59050 in contig BA000014_GR.
KEGG	ath:AT3G59050.
NMPDR	fig|3702.1.peg.17251.
Organism-specific databases
TAIR	At3g59050.
Phylogenomic databases
eggNOG	KOG0029.
HOGENOM	HBG543533.
InParanoid	Q9LYT1.
OMA	KEACISS.
PhylomeDB	Q9LYT1.
Gene expression databases
Genevestigator	Q9LYT1.
Family and domain databases
InterPro	IPR001613. Amineoxid_fl. IPR002937. Amino_oxidase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
PRINTS	PR00757. AMINEOXDASEF.
ProtoNet	Search...

Entry information

Entry name

PAO3_ARATH

Accession

Primary (citable) accession number: Q9LYT1
Secondary accession number(s): Q8LE44

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)