PAO7_ORYSJ
ID PAO7_ORYSJ Reviewed; 474 AA.
AC Q0J290; Q6H5M6;
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 7 {ECO:0000303|PubMed:24634478};
DE Short=OsPAO7 {ECO:0000303|PubMed:24634478};
DE EC=1.5.3.- {ECO:0000269|PubMed:24634478};
DE Flags: Precursor;
GN Name=PAO7 {ECO:0000303|PubMed:24634478};
GN OrderedLocusNames=Os09g0368500 {ECO:0000312|EMBL:BAT07750.1},
GN LOC_Os09g20284 {ECO:0000305};
GN ORFNames=OSNPB_090368500 {ECO:0000312|EMBL:BAT07750.1};
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=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 [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=24634478; DOI=10.1093/pcp/pcu047;
RA Liu T., Kim D.W., Niitsu M., Maeda S., Watanabe M., Kamio Y., Berberich T.,
RA Kusano T.;
RT "Polyamine oxidase 7 is a terminal catabolism-type enzyme in Oryza sativa
RT and is specifically expressed in anthers.";
RL Plant Cell Physiol. 55:1110-1122(2014).
CC -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion
CC (PubMed:24634478). Catalyzes the oxidation of the secondary amino group
CC of polyamines, such as spermine, spermidine and their acetyl
CC derivatives (PubMed:24634478). Substrate preference is spermine >
CC spermidine > N(1)-acetylspermine > N(1)-acetylspermidine > norspermine
CC > thermospermine (PubMed:24634478). No activity detected when
CC putrescine is used as substrate (PubMed:24634478). May play a role in
CC producing hydrogen peroxide for secondary wall thickening through
CC lignin formation during anther development (Probable).
CC {ECO:0000269|PubMed:24634478, ECO:0000305|PubMed:24634478}.
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:24634478};
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:24634478};
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:24634478};
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:24634478};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermidine + O2 = 3-acetamidopropanal + H2O2
CC + putrescine; Xref=Rhea:RHEA:25812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:58324, ChEBI:CHEBI:326268;
CC Evidence={ECO:0000269|PubMed:24634478};
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:24634478};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:24634478};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:24634478};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38.3 uM for spermine (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:24634478};
CC KM=59.4 uM for N(1)-acetylspermine (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:24634478};
CC KM=75 uM for thermospermine (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:24634478};
CC KM=78.8 uM for norspermine (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:24634478};
CC KM=42.2 uM for spermidine (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24634478};
CC KM=80.3 uM for N(1)-acetylspermidine (at pH 7.0 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:24634478};
CC KM=108.8 uM for norspermidine (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24634478};
CC pH dependence:
CC Optimum pH is 7.0 with spermidine as substrate (PubMed:24634478).
CC Optimum pH is 6.5 with spermine as substrate (PubMed:24634478).
CC {ECO:0000269|PubMed:24634478};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius with spermidine as
CC substrate (PubMed:24634478). Optimum temperature is 30 degrees
CC Celsius with spermine as substrate (PubMed:24634478).
CC {ECO:0000269|PubMed:24634478};
CC -!- PATHWAY: Amine and polyamine degradation; spermidine degradation.
CC {ECO:0000305}.
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:24634478}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed during anther development,
CC from the meiosis/tetrad pollen stage to the tricellular pollen stage,
CC with a peak at the bicellular pollen stage.
CC {ECO:0000269|PubMed:24634478}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD25916.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD25973.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP005525; BAD25916.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP005580; BAD25973.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008215; BAF24925.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT07750.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0J290; -.
DR SMR; Q0J290; -.
DR STRING; 4530.OS09T0368500-01; -.
DR PaxDb; Q0J290; -.
DR PRIDE; Q0J290; -.
DR EnsemblPlants; Os09t0368500-01; Os09t0368500-01; Os09g0368500.
DR Gramene; Os09t0368500-01; Os09t0368500-01; Os09g0368500.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_6_1_1; -.
DR InParanoid; Q0J290; -.
DR OMA; MKFADNY; -.
DR BRENDA; 1.5.3.14; 4460.
DR PlantReactome; R-OSA-1119567; Beta-alanine biosynthesis I.
DR UniPathway; UPA00211; -.
DR UniPathway; UPA00250; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0052904; F:N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; 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: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: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 Apoplast; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..474
FT /note="Polyamine oxidase 7"
FT /id="PRO_5013530428"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 261
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 454
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 474 AA; 53258 MW; 6D8324200D3D5F87 CRC64;
MTKPTTMAIF LSIVLLSMAQ LPSLVAGTGR PRVIIIGAGI SGISAGKRLS EAGITDILIL
EATDHIGGRM HKQRFAGVNV EIGANWVEGV NGEKMNPIWP IVNSTLKLRN FLSDFDSLAQ
NVYKDGGLCD AAYVQKRIDL ADEADKSGEN LSATLHPSGR DDMSILSMQR LNNHLPNGPS
SPVDMVVDYF TYDYEFAEPP RVTSLRNTVP LPTFTDFGDD NYFVADQRGY EAVVYYLAGQ
YLEADKSGNI VDARLQLNKV VREISYSSTG VTVKTEDNST YQADYVMVSA SLGVLQSDLI
QFKPQLPSWK ILAIYQFDMA VYTKIFVKFP KKFWPEGAGR EFFLYASTRR GYYGVWQEFE
KQYPDANVLL VTVTDEESRR IEQQPDSQTK AEIMEVVRSM FPDEDVPDAT DILVPRWWSD
RFFQGSFSNW PIGVSRYEHD QLRAPVGRVY FTGEHTSERY NGYVHGAYLA GIYA
