PAO5_ORYSJ
ID PAO5_ORYSJ Reviewed; 492 AA.
AC Q0J954; Q7XPI8;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Polyamine oxidase 5 {ECO:0000303|PubMed:21796433};
DE Short=OsPAO5 {ECO:0000303|PubMed:21796433};
DE EC=1.5.3.- {ECO:0000269|PubMed:21796433};
GN Name=PAO5 {ECO:0000303|PubMed:21796433};
GN OrderedLocusNames=Os04g0671300 {ECO:0000312|EMBL:BAF16133.1},
GN LOC_Os04g57560 {ECO:0000305};
GN ORFNames=OsJ_16579 {ECO:0000312|EMBL:EEE61884.1},
GN OSJNBb0004A17.1 {ECO:0000312|EMBL:CAE03599.2};
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 [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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
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).
RN [8]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=27570530; DOI=10.3389/fpls.2016.01219;
RA Chen B.X., Li W.Y., Gao Y.T., Chen Z.J., Zhang W.N., Liu Q.J., Chen Z.,
RA Liu J.;
RT "Involvement of polyamine oxidase-produced hydrogen peroxide during
RT coleorhiza-limited germination of rice seeds.";
RL Front. Plant Sci. 7:1219-1219(2016).
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 (PubMed:21796433). Substrate preference
CC is spermine > thermospermine > norspermine (PubMed:21796433). No
CC activity detected when putrescine, spermidine or N(1)-acetylspermidine
CC are used as substrates (PubMed:21796433). Plays an important role in
CC the regulation of polyamine intracellular concentration (Probable). May
CC play a role in producing hydrogen peroxide during seed germination
CC (Probable). {ECO:0000269|PubMed:21796433, ECO:0000305|PubMed:21796433,
CC ECO:0000305|PubMed:27570530}.
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 + 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 + 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 -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:21796433}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21796433}.
CC -!- DEVELOPMENTAL STAGE: During seed germination, expression increases in
CC the embryo from 3 to 48 hours after seed imbition, with a peak at 48
CC hours. {ECO:0000269|PubMed:27570530}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE03599.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL606652; CAE03599.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF16133.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91567.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE61884.1; -; Genomic_DNA.
DR EMBL; AK072414; BAG92960.1; -; mRNA.
DR RefSeq; XP_015636452.1; XM_015780966.1.
DR AlphaFoldDB; Q0J954; -.
DR SMR; Q0J954; -.
DR STRING; 4530.OS04T0671300-01; -.
DR PaxDb; Q0J954; -.
DR PRIDE; Q0J954; -.
DR EnsemblPlants; Os04t0671300-01; Os04t0671300-01; Os04g0671300.
DR GeneID; 4337360; -.
DR Gramene; Os04t0671300-01; Os04t0671300-01; Os04g0671300.
DR KEGG; osa:4337360; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_10_0_1; -.
DR InParanoid; Q0J954; -.
DR OMA; GGQWIGH; -.
DR OrthoDB; 1034142at2759; -.
DR UniPathway; UPA00211; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IDA:UniProtKB.
DR GO; GO:0006598; P:polyamine catabolic process; IBA:GO_Central.
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..492
FT /note="Polyamine oxidase 5"
FT /id="PRO_0000445724"
FT MOTIF 490..492
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 244
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 431
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
SQ SEQUENCE 492 AA; 54186 MW; CD7603D222CDEEFD CRC64;
MDQPSNGFAA GGLFLRHIDG QNASPPSVIV IGGGISGIAA ARALSNASFK VTLLESRDRL
GGRVHTDYSF GCPIDMGASW LHGVCNENSL APLIRLLGLR LYRTSGDNSV LYDHDLESYA
LFDKDGRQVP QEIVTKVGET FEKILKETVK VRAEHEDDMP LIQAISIVLD RNPHLKLDGL
QYEVLQWCIC RLEAWFATDV DNISLKNWDQ EHVLTGGHGL MVHGYDPVIK ALAQDLDIHL
NHRVTKIIQR YNKTIVCVED GTSFVADAAI ITVPLGVLKA NIIKFEPELP DWKLSSISDL
GIGIENKIAL RFNSVFWPNV EVLGRVAPTS NACGYFLNLH KATGHPVLVC MVAGRFAYEF
EKLSDEESVN FVMSQLKKML PGATEPVQYL VSRWGTDPNS LGSYSCDLVG KPADLYERFC
APVGNLFFAG EAACIDHSGS VHGAYSSGIV AAEDCRRHLS TQLGISDLFQ VGKIIMREEM
TEVMVPFQIS RL
