PAO6_ORYSJ
ID PAO6_ORYSJ Reviewed; 496 AA.
AC A0A0P0XM10; Q0J291; Q6H5M8;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Polyamine oxidase 6 {ECO:0000303|PubMed:28786735};
DE Short=OsPAO6 {ECO:0000303|PubMed:28786735};
DE EC=1.5.3.- {ECO:0000250|UniProtKB:Q0J290};
DE AltName: Full=Polyamine oxidase B;
DE Flags: Precursor;
GN Name=PAO6 {ECO:0000303|PubMed:28786735};
GN Synonyms=PAOB {ECO:0000303|PubMed:20472577};
GN OrderedLocusNames=Os09g0368200 {ECO:0000312|EMBL:BAT07747.1},
GN LOC_Os09g20260 {ECO:0000305};
GN ORFNames=OJ1759_F09.3 {ECO:0000312|EMBL:BAD25971.1},
GN P0564H06.9 {ECO:0000312|EMBL:BAD25914.1};
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 [MRNA], SUBCELLULAR LOCATION, AND INDUCTION BY
RP JASMONATE.
RC STRAIN=cv. Nipponbare;
RX PubMed=28786735; DOI=10.1080/15592324.2017.1359456;
RA Sagor G.H.M., Kusano T., Berberich T.;
RT "Identification of the actual coding region for polyamine oxidase 6 from
RT rice (OsPAO6) and its partial characterization.";
RL Plant Signal. Behav. 12:E1359456-E1359456(2017).
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 INDUCTION BY SALT STRESS.
RX PubMed=20472577; DOI=10.1093/jxb/erq118;
RA Quinet M., Ndayiragije A., Lefevre I., Lambillotte B., Dupont-Gillain C.C.,
RA Lutts S.;
RT "Putrescine differently influences the effect of salt stress on polyamine
RT metabolism and ethylene synthesis in rice cultivars differing in salt
RT resistance.";
RL J. Exp. Bot. 61:2719-2733(2010).
CC -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion (By
CC similarity). Catalyzes the oxidation of the secondary amino group of
CC polyamines, such as spermine and spermidine (By similarity).
CC {ECO:0000250|UniProtKB:Q0J290}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q0J290};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q0J290};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:28786735}.
CC -!- INDUCTION: Induced by salt stress in shoots and roots
CC (PubMed:20472577). Induced by treatment with jasmonate
CC (PubMed:28786735). {ECO:0000269|PubMed:20472577,
CC ECO:0000269|PubMed:28786735}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD25914.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD25971.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF24924.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; LC107620; BAV17937.1; -; mRNA.
DR EMBL; AP005525; BAD25914.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP005580; BAD25971.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008215; BAF24924.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014965; BAT07747.1; -; Genomic_DNA.
DR RefSeq; XP_015611019.1; XM_015755533.1.
DR AlphaFoldDB; A0A0P0XM10; -.
DR SMR; A0A0P0XM10; -.
DR STRING; 4530.OS09T0368200-00; -.
DR PaxDb; A0A0P0XM10; -.
DR EnsemblPlants; Os09t0368200-00; Os09t0368200-00; Os09g0368200.
DR GeneID; 4346881; -.
DR Gramene; Os09t0368200-00; Os09t0368200-00; Os09g0368200.
DR KEGG; osa:4346881; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_6_1_1; -.
DR OMA; SFRSYWE; -.
DR OrthoDB; 508351at2759; -.
DR PlantReactome; R-OSA-1119567; Beta-alanine biosynthesis I.
DR UniPathway; UPA00211; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016647; F:oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor; IEA:UniProt.
DR GO; GO:0046208; P:spermine catabolic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Apoplast; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..496
FT /note="Polyamine oxidase 6"
FT /id="PRO_5013461417"
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 496 AA; 55654 MW; D381E47D8D6B7090 CRC64;
MTKPTTMAIF LVLALSIAQL LPSLVAGTGR PRVIIVGAGI SGISAGKRIW EAGIADVLIL
EATDRIGGRM HKQSFAGVNV EIGANWVEGV NGEKKNPIWP IVNSTLKLRS FRSDFDSLAQ
NVYKDGGLCD EAYVQKRMDR ADEVDKSGEN LSATLHPSGR DDMSILSMQR LNDHLPNGPS
SPVDMAVDYF TYDYEFAEPP RVTSLQNTVP LPTFTDFGDD TYFVADQRGY ESVVHHLAGQ
YLNADKSGNI ADARLKLNKV VREISYSSTG VTVKTEDNST YQADYVMVSA SLGVLQSDLI
QFKPQLPSWK ILAIYQFDMA VYTKIFVKFP KKFWPEGAGR EFFLYASTRR GYYGVWQEFE
KQYPDANVLL VTVTDEESRR IEQQPDSQTK AEIMEVVRCM FPDEDVPDAT DILVPRWWSD
RFFRGSFSNW PIGVSRYEYD QLRAPVGRVY FTGEHTSERY NGYVHGAYLA GIDSAEILIN
CAQKKMCKYN VGGKHG
