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Q9LYT1 (PAO3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyamine oxidase 3
Short name=AtPAO3
EC=1.5.3.17
Gene names
Name:PAO3
Ordered Locus Names:At3g59050
ORF Names:F17J16.100
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceEvidence 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.7

Catalytic activity

Spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2. Ref.7

Spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2. Ref.7

N(1)-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2. Ref.7

N(1)-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2. Ref.7

Cofactor

Binds 1 FAD per subunit.

Enzyme regulation

Inhibited by guazatine, aminoguanidine and putrescine. Ref.7

Pathway

Amine and polyamine degradation; spermine degradation.

Subcellular location

Peroxisome Ref.6 Ref.7.

Tissue specificity

Expressed at similar levels in all tissues tested. Highest expression is seen in siliques. Ref.7

Induction

By abscisic acid, jasmonate, salicylic acid, wounding and flagellin 22, a pathogen elicitor. Ref.7

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.204 mM for spermidine Ref.7

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 componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpolyamine catabolic process

Inferred from direct assay Ref.7. Source: TAIR

   Cellular componentperoxisome

Inferred from direct assay Ref.7. Source: TAIR

   Molecular functionpolyamine oxidase activity

Inferred from direct assay Ref.7. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Polyamine oxidase 3
PRO_0000352509

Experimental info

Sequence conflict2471I → V in AAM62855. Ref.4
Sequence conflict3661K → N in AAM62855. Ref.4
Sequence conflict4041L → M in AAM62855. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9LYT1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1EC37D18794A2BD4

FASTA48854,132
        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

« Hide

References

« Hide '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. expand/collapse author list , 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]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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.
[4]"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].
[5]"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.
[6]"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.
[7]"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.
CP002686 Genomic DNA. Translation: AEE79866.1.
AY065025 mRNA. Translation: AAL57665.1.
AY143905 mRNA. Translation: AAN28844.1.
AY085634 mRNA. Translation: AAM62855.1.
IPIIPI00545156.
PIRT47787.
RefSeqNP_191464.1. NM_115767.3.
UniGeneAt.27590.

3D structure databases

HSSPHSSP built from PDB template 1RSG based on UniProtKB P50264.
ProteinModelPortalQ9LYT1.
SMRQ9LYT1. Positions 29-465.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9LYT1. 1 interaction.

Proteomic databases

PRIDEQ9LYT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G59050.1; AT3G59050.1; AT3G59050.
GeneID825074.
GenomeReviewsGene locus AT3G59050 in contig BA000014_GR.
KEGGath:AT3G59050.
NMPDRfig|3702.1.peg.17251.

Organism-specific databases

TAIRAt3g59050.

Phylogenomic databases

eggNOGKOG0029.
GeneTreeEPGT00070000028232.
HOGENOMHBG543533.
InParanoidQ9LYT1.
OMAMEEEAPA.
PhylomeDBQ9LYT1.
ProtClustDBPLN02268.

Enzyme and pathway databases

BioCycARA:AT3G59050-MONOMER.
MetaCyc:AT3G59050-MONOMER.

Gene expression databases

GenevestigatorQ9LYT1.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
KOK13367.
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Entry information

Entry namePAO3_ARATH
AccessionPrimary (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: December 14, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents