PAO1_ORYSJ
ID PAO1_ORYSJ Reviewed; 512 AA.
AC Q5NAI7;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Polyamine oxidase 1 {ECO:0000303|PubMed:24105034};
DE Short=OsPAO1 {ECO:0000303|PubMed:24105034};
DE EC=1.5.3.- {ECO:0000269|PubMed:24105034};
DE AltName: Full=OsAO4 {ECO:0000305};
GN Name=PAO1 {ECO:0000303|PubMed:24105034};
GN OrderedLocusNames=Os01g0710200 {ECO:0000312|EMBL:BAF05952.1},
GN LOC_Os01g51320 {ECO:0000305};
GN ORFNames=OsJ_03212 {ECO:0000312|EMBL:EAZ13287.1},
GN P0456F08.19 {ECO:0000312|EMBL:BAD81522.1};
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=24105034; DOI=10.1007/s00299-013-1518-y;
RA Liu T., Kim D.W., Niitsu M., Berberich T., Kusano T.;
RT "Oryza sativa polyamine oxidase 1 back-converts tetraamines, spermine and
RT thermospermine, to spermidine.";
RL Plant Cell Rep. 33:143-151(2014).
CC -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion
CC (PubMed:24105034). Catalyzes the oxidation of the secondary amino group
CC of polyamines, such as spermine and its acetyl derivatives
CC (PubMed:24105034). Substrate preference is thermospermine > spermine >
CC norspermine > N(1)-acetylspermine (PubMed:24105034). No activity
CC detected when putrescine or spermidine are used as substrates
CC (PubMed:24105034). Plays an important role in the regulation of
CC polyamine intracellular concentration (Probable).
CC {ECO:0000269|PubMed:24105034, ECO:0000305|PubMed:24105034}.
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:24105034};
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:24105034};
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:24105034};
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:24105034};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:24105034};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:24105034};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.69 uM for thermospermine (at pH 6.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:24105034};
CC KM=4.93 uM for spermine (at pH 6.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:24105034};
CC KM=10.93 uM for norspermine (at pH 6.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:24105034};
CC pH dependence:
CC Optimum pH is 6.0 with thermospermine as substrate (PubMed:24105034).
CC Optimum pH is 8.5 with spermine as substrate (PubMed:24105034).
CC {ECO:0000269|PubMed:24105034};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius with thermospermine as
CC substrate (PubMed:24105034). Optimum temperature is 35 degrees
CC Celsius with spermine as substrate (PubMed:24105034).
CC {ECO:0000269|PubMed:24105034};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24105034}.
CC -!- INDUCTION: Induced in roots by exogenous treatment with spermine and
CC thermospermine. {ECO:0000269|PubMed:24105034}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AP002901; BAD81522.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF05952.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS73974.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ13287.1; -; Genomic_DNA.
DR RefSeq; XP_015630114.1; XM_015774628.1.
DR AlphaFoldDB; Q5NAI7; -.
DR SMR; Q5NAI7; -.
DR STRING; 4530.OS01T0710200-00; -.
DR PaxDb; Q5NAI7; -.
DR PRIDE; Q5NAI7; -.
DR EnsemblPlants; Os01t0710200-01; Os01t0710200-01; Os01g0710200.
DR GeneID; 4327828; -.
DR Gramene; Os01t0710200-01; Os01t0710200-01; Os01g0710200.
DR KEGG; osa:4327828; -.
DR eggNOG; KOG0685; Eukaryota.
DR HOGENOM; CLU_004498_2_3_1; -.
DR InParanoid; Q5NAI7; -.
DR OMA; IPKPHKV; -.
DR OrthoDB; 508351at2759; -.
DR PlantReactome; R-OSA-1119567; Beta-alanine biosynthesis I.
DR UniPathway; UPA00211; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; 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:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IDA:UniProtKB.
DR GO; GO:1990534; F:thermospermine oxidase activity; IEA:EnsemblPlants.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IEA:EnsemblPlants.
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 Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..512
FT /note="Polyamine oxidase 1"
FT /id="PRO_0000445721"
FT REGION 448..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 476
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
SQ SEQUENCE 512 AA; 54112 MW; B73C87D3C909927B CRC64;
MVAKKPRVVV VGAGISGLAA AHRLCGAGGD RFEVAVVEAG DRVGGRILTS EFAGHRVEMG
ATWVQGVVGS PVYALARDAG ALGEEEGRGL PYERMDGFPD RVLTVAEGGE VVDADTVAGP
IEELYRGMME AARAGEAGGG GGVEEYLRRG LRAYQAARSA GGGGGGGKEL EEVDEALLAM
HINRERTDTS ADDLGDLDLT AEGEYRDFPG EHVTIPGGYS RVVERLAAAL PPGTVRLGLR
LRRLKWGGTP VRLHFADGAP PLTADHVILT VSLGVLKASL GNKDTAGVGA AAIAFDPPLP
PFKREAVARL GFGVVNKLFM EVEAVAPSEP EDVAGVQPAA AGFPFLHMAF RGHVSKIPWW
MRGTESICPV HAGSTVALAW FAGREAAHLE SLPDDDVIRG AHATLDSFLP AAPRWRVRRI
KRSGWATDPL FLGSYSYVAV GSSGDDLDRM AEPLPRGPDA AADERPPSPR LLFAGEATHR
THYSTTHAAY LSGVREANRL LQHYRGGANH TT
