PAO3_ORYSJ
ID PAO3_ORYSJ Reviewed; 484 AA.
AC Q7X809; I4DI81;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Polyamine oxidase 3 {ECO:0000303|PubMed:21796433};
DE Short=OsPAO3 {ECO:0000303|PubMed:21796433};
DE EC=1.5.3.- {ECO:0000269|PubMed:21796433};
GN Name=PAO3 {ECO:0000303|PubMed:21796433};
GN OrderedLocusNames=Os04g0623300 {ECO:0000312|EMBL:BAF15837.1},
GN LOC_Os04g53190 {ECO:0000305};
GN ORFNames=OsJ_16215 {ECO:0000312|EMBL:EEE61715.1},
GN OSJNBa0053K19.6 {ECO:0000312|EMBL:CAE03498.2},
GN OSJNBb0085C12.17 {ECO:0000312|EMBL:CAD41837.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Katsuyuki I., Kuboyama T., Matsumoto T., Wu J., Kanamori H.;
RT "Oryza sativa japonica group DNA, complete sequence, cultivar: Jamaica.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21796433; DOI=10.1007/s00726-011-1002-3;
RA Ono Y., Kim D.W., Watanabe K., Sasaki A., Niitsu M., Berberich T.,
RA Kusano T., Takahashi Y.;
RT "Constitutively and highly expressed Oryza sativa polyamine oxidases
RT localize in peroxisomes and catalyze polyamine back conversion.";
RL Amino Acids 42:867-876(2012).
CC -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion
CC (PubMed:21796433). Catalyzes the oxidation of the secondary amino group
CC of polyamines, such as spermine, spermidine and their acetyl
CC derivatives (PubMed:21796433). Substrate preference is spermidine >
CC norspermine > thermospermine > N(1)-acetylspermine > spermine
CC (PubMed:21796433). No activity detected when putrescine is used as
CC substrate (PubMed:21796433). Plays an important role in the regulation
CC of polyamine intracellular concentration (Probable).
CC {ECO:0000269|PubMed:21796433, ECO:0000305|PubMed:21796433}.
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:21796433};
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:21796433};
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:21796433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + spermidine = 3-aminopropanal + H2O2 + putrescine;
CC Xref=Rhea:RHEA:25808, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:57834, ChEBI:CHEBI:58374,
CC ChEBI:CHEBI:326268; Evidence={ECO:0000269|PubMed:21796433};
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:21796433};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:21796433};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:21796433};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305}.
CC -!- PATHWAY: Amine and polyamine degradation; spermidine degradation.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:21796433}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21796433}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAM17621.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP011523; BAM17621.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL606660; CAD41837.2; -; Genomic_DNA.
DR EMBL; AL606645; CAE03498.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF15837.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91077.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE61715.1; -; Genomic_DNA.
DR RefSeq; XP_015636130.1; XM_015780644.1.
DR AlphaFoldDB; Q7X809; -.
DR SMR; Q7X809; -.
DR STRING; 4530.OS04T0623300-01; -.
DR PaxDb; Q7X809; -.
DR PRIDE; Q7X809; -.
DR EnsemblPlants; Os04t0623300-01; Os04t0623300-01; Os04g0623300.
DR GeneID; 4337046; -.
DR Gramene; Os04t0623300-01; Os04t0623300-01; Os04g0623300.
DR KEGG; osa:4337046; -.
DR eggNOG; KOG0029; Eukaryota.
DR InParanoid; Q7X809; -.
DR OMA; EFFDNYQ; -.
DR OrthoDB; 1034142at2759; -.
DR UniPathway; UPA00211; -.
DR UniPathway; UPA00250; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q7X809; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0052903; F:N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IDA:UniProtKB.
DR GO; GO:0052894; F:norspermine:oxygen oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase activity; IBA:GO_Central.
DR GO; GO:0052902; F:spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity; IEA:RHEA.
DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IDA:UniProtKB.
DR GO; GO:0006598; P:polyamine catabolic process; IBA:GO_Central.
DR GO; GO:0046203; P:spermidine catabolic process; IDA:UniProtKB.
DR GO; GO:0046208; P:spermine catabolic process; IDA:UniProtKB.
DR GO; GO:1903602; P:thermospermine catabolic process; IDA:UniProtKB.
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; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..484
FT /note="Polyamine oxidase 3"
FT /id="PRO_0000445722"
FT MOTIF 482..484
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 423
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
SQ SEQUENCE 484 AA; 53644 MW; 9B81B8B10B04BC33 CRC64;
MANNSSYGEN VRRKSHTPSA IVIGSGFAGI AAANALRNAS FEVVLLESRD RIGGRIHTDY
SFGFPVDLGA SWLHGVCEEN PLAPIIGRLG LPLYRTSGDD SVLFDHDLES YALYDTKGHQ
VPQELVEKIG KVFETILEET GKLREETKED ISIAKAIAIV MERNPHLRQE GIAHDVLQWY
LCRMEGWFAT DADAISLQGW DQEVLLPGGH GLMVRGYRPV INTLAKGLDI RLGHRVVEIV
RHRNRVEVTV SSGKTFVADA AVIAVPLGVL KANTIKFEPR LPEWKEEAIR ELSVGVENKI
ILHFSEVFWP NVEFLGVVSS TTYGCSYFLN LHKATGHPVL VYMPAGRLAC DIEKLSDEAA
AQFAFSQLKK ILPNAAEPIH YLVSHWGSDE NTLGSYTFDG VGKPRDLYEK LRIPVDNLFF
AGEATSVQYT GTVHGAFSTG LMAAEECRMR VLERFRELDM LEMCHPAMGE QTATVSVPLL
ISRL
