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Polyamine oxidase 1 (AtPAO1) (EC 1.5.3.16) (N(1)-acetylpolyamine oxidase) (Spermine oxidase)

 PAO1_ARATH              Reviewed;         472 AA.
Q9FNA2; Q7FL79;
14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 107.
RecName: Full=Polyamine oxidase 1;
Short=AtPAO1;
EC=1.5.3.16;
AltName: Full=N(1)-acetylpolyamine oxidase;
AltName: Full=Spermine oxidase;
Name=PAO1; Synonyms=PAO; OrderedLocusNames=At5g13700;
ORFNames=MSH12.17;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9405937; DOI=10.1093/dnares/4.4.291;
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. II.
Sequence features of the regions of 1,044,062 bp covered by thirteen
physically assigned P1 clones.";
DNA Res. 4:291-300(1997).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[5]
IDENTIFICATION.
PubMed=11432750; DOI=10.1046/j.1432-1327.2001.02296.x;
Cervelli M., Cona A., Angelini R., Polticelli F., Federico R.,
Mariottini P.;
"A barley polyamine oxidase isoform with distinct structural features
and subcellular localization.";
Eur. J. Biochem. 268:3816-3830(2001).
[6]
FUNCTION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16778015; DOI=10.1104/pp.106.080911;
Tavladoraki P., Rossi M.N., Saccuti G., Perez-Amador M.A.,
Polticelli F., Angelini R., Federico R.;
"Heterologous expression and biochemical characterization of a
polyamine oxidase from Arabidopsis involved in polyamine back
conversion.";
Plant Physiol. 141:1519-1532(2006).
-!- FUNCTION: Flavoenzyme that catalyzes the oxidation of the
secondary amino group of spermine, norspermine and N(1)-
acetylspermine. Substrate preference is norspermine > spermine >
N(1)-acetylspermine. No activity detected when putrescine,
spermidine or N(1)-acetylspermidine are used as substrates. Plays
an important role in the regulation of polyamine intracellular
concentration. {ECO:0000269|PubMed:16778015}.
-!- CATALYTIC ACTIVITY: Spermine + O(2) + H(2)O = spermidine + 3-
aminopropanal + H(2)O(2).
-!- CATALYTIC ACTIVITY: Spermidine + O(2) + H(2)O = putrescine + 3-
aminopropanal + H(2)O(2).
-!- CATALYTIC ACTIVITY: N(1)-acetylspermine + O(2) + H(2)O =
spermidine + 3-acetamidopropanal + H(2)O(2).
-!- CATALYTIC ACTIVITY: Norspermine + O(2) + H(2)O = norspermidine +
3-aminopropanal + H(2)O(2).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD per subunit.;
-!- ENZYME REGULATION: Inhibited by guazatine, N-prenylagmatine and
1,12-diaminododecane.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.11 mM for spermine {ECO:0000269|PubMed:16778015};
KM=0.09 mM for norspermine {ECO:0000269|PubMed:16778015};
KM=0.2 mM for N(1)-acetylspermine {ECO:0000269|PubMed:16778015};
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:16778015};
-!- PATHWAY: Amine and polyamine degradation; spermine degradation.
-!- TISSUE SPECIFICITY: Expressed at very low levels in leaves, stems
and inflorescences. {ECO:0000269|PubMed:16778015}.
-!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB006704; BAB08697.1; -; Genomic_DNA.
EMBL; CP002688; AED91929.1; -; Genomic_DNA.
EMBL; AK118627; BAC43225.2; -; mRNA.
EMBL; BT026370; ABH04477.1; -; mRNA.
RefSeq; NP_196874.1; NM_121373.4.
UniGene; At.49017; -.
UniGene; At.6477; -.
ProteinModelPortal; Q9FNA2; -.
SMR; Q9FNA2; -.
BioGrid; 16493; 1.
STRING; 3702.AT5G13700.1; -.
PaxDb; Q9FNA2; -.
EnsemblPlants; AT5G13700.1; AT5G13700.1; AT5G13700.
GeneID; 831215; -.
Gramene; AT5G13700.1; AT5G13700.1; AT5G13700.
KEGG; ath:AT5G13700; -.
Araport; AT5G13700; -.
TAIR; locus:2173219; AT5G13700.
eggNOG; KOG0029; Eukaryota.
eggNOG; ENOG410XSNC; LUCA.
HOGENOM; HOG000174927; -.
InParanoid; Q9FNA2; -.
KO; K13366; -.
OMA; MGAQFIN; -.
OrthoDB; EOG09360ACK; -.
PhylomeDB; Q9FNA2; -.
BioCyc; ARA:AT5G13700-MONOMER; -.
BioCyc; MetaCyc:AT5G13700-MONOMER; -.
BRENDA; 1.5.3.16; 399.
UniPathway; UPA00211; -.
PRO; PR:Q9FNA2; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FNA2; baseline and differential.
Genevisible; Q9FNA2; AT.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:TAIR.
GO; GO:0052895; F:N1-acetylspermine:oxygen oxidoreductase (N1-acetylspermidine-forming) activity; IEA:UniProtKB-EC.
GO; GO:0052894; F:norspermine:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
GO; GO:0046592; F:polyamine oxidase activity; IDA:TAIR.
GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC.
GO; GO:0006598; P:polyamine catabolic process; IDA:TAIR.
GO; GO:0046208; P:spermine catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.50.50.60; -; 3.
InterPro; IPR002937; Amino_oxidase.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR001613; Flavin_amine_oxidase.
Pfam; PF01593; Amino_oxidase; 2.
PRINTS; PR00757; AMINEOXDASEF.
SUPFAM; SSF51905; SSF51905; 2.
1: Evidence at protein level;
Complete proteome; FAD; Flavoprotein; Oxidoreductase;
Reference proteome.
CHAIN 1 472 Polyamine oxidase 1.
/FTId=PRO_0000352507.
CONFLICT 21 21 V -> I (in Ref. 3; BAC43225).
{ECO:0000305}.
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


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