PAO4_ORYSJ
ID PAO4_ORYSJ Reviewed; 487 AA.
AC Q7XR46;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Polyamine oxidase 4 {ECO:0000303|PubMed:21796433};
DE Short=OsPAO4 {ECO:0000303|PubMed:21796433};
DE EC=1.5.3.- {ECO:0000269|PubMed:21796433};
GN Name=PAO4 {ECO:0000303|PubMed:21796433};
GN OrderedLocusNames=Os04g0671200 {ECO:0000312|EMBL:BAF16132.1},
GN LOC_Os04g57550 {ECO:0000305};
GN ORFNames=OsJ_16578 {ECO:0000312|EMBL:EAZ32367.1},
GN OSJNBa0043A12.39 {ECO:0000312|EMBL:CAE02834.1};
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=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 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 (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).
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 + 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 -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AL606619; CAE02834.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF16132.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91564.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ32367.1; -; Genomic_DNA.
DR RefSeq; XP_015637015.1; XM_015781529.1.
DR AlphaFoldDB; Q7XR46; -.
DR SMR; Q7XR46; -.
DR STRING; 4530.OS04T0671200-01; -.
DR PaxDb; Q7XR46; -.
DR PRIDE; Q7XR46; -.
DR EnsemblPlants; Os04t0671200-01; Os04t0671200-01; Os04g0671200.
DR GeneID; 4337359; -.
DR Gramene; Os04t0671200-01; Os04t0671200-01; Os04g0671200.
DR KEGG; osa:4337359; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_10_0_1; -.
DR InParanoid; Q7XR46; -.
DR OMA; GFGTCNK; -.
DR OrthoDB; 1034142at2759; -.
DR UniPathway; UPA00211; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q7XR46; 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: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..487
FT /note="Polyamine oxidase 4"
FT /id="PRO_0000445723"
FT MOTIF 485..487
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 242
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 429
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
SQ SEQUENCE 487 AA; 52913 MW; 5D2F87FAF8CE589F CRC64;
MDPNSLKTGG LLLPTIERQC ASPPSVIVIG GGISGVAAAR ALSNASFEVT VLESRDRVGG
RVHTDYSFGC PIDMGASWLH GVCNENSLAP LIGYLGLKLY RTSGDNSVLY DHDLESYALF
DKAGHQVSKE TVAKVEETFE RILDETVKVR DEQEHDMPLL QAISLVLERH PHLKLQGIDD
QVLQWCVCRL EAWFAADADE ISLKNWDQEH VLTGGHGLMV NGYYPIIQAL AQGLDIRLNQ
RVTKIARQFN GVTVTTEDGT SYSADACIIT VPLGVLKANI IKFEPELPSW KSSAIADLGV
GIENKIAMHF DTVFWPNVEV LGMVGPTPKA CGYFLNLHKA TGNPVLVYMA AGRFAQEVEK
LSDKEAVDLV MSHLKKMLPD ATEPTKYLVS RWGSDPNSLG SYSCDLVGKP ADVSARFAAP
VENLYFAGEA ASADHSGSVH GAYSSGIAAA DECRKRILMQ KGIPDLVQVK AYEEMAGVIA
PLQICRT
