PAO4_ARATH
ID PAO4_ARATH Reviewed; 497 AA.
AC Q8H191; Q94JZ7; Q9SHX4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable polyamine oxidase 4 {ECO:0000303|PubMed:18703589};
DE Short=AtPAO4 {ECO:0000303|PubMed:18703589};
DE EC=1.5.3.16 {ECO:0000269|PubMed:18703589};
DE AltName: Full=Amine oxidase 2 {ECO:0000312|EMBL:AAO85405.1};
GN Name=PAO4; OrderedLocusNames=At1g65840 {ECO:0000312|Araport:AT1G65840};
GN ORFNames=F1E22.18 {ECO:0000312|EMBL:AAF23834.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta;
RA Pinontoan R., Cunningham K.W., Iida H., Uozumi N., Muto S.;
RT "A putative amine oxidase 2 from Arabidopsis.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION.
RX PubMed=16778015; DOI=10.1104/pp.106.080911;
RA Tavladoraki P., Rossi M.N., Saccuti G., Perez-Amador M.A., Polticelli F.,
RA Angelini R., Federico R.;
RT "Heterologous expression and biochemical characterization of a polyamine
RT oxidase from Arabidopsis involved in polyamine back conversion.";
RL Plant Physiol. 141:1519-1532(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=18703589; DOI=10.1093/pcp/pcn114;
RA Kamada-Nobusada T., Hayashi M., Fukazawa M., Sakakibara H., Nishimura M.;
RT "A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine
RT catabolism in Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:1272-1282(2008).
RN [7]
RP INDUCTION.
RX PubMed=18583528; DOI=10.1104/pp.108.123802;
RA Moschou P.N., Sanmartin M., Andriopoulou A.H., Rojo E.,
RA Sanchez-Serrano J.J., Roubelakis-Angelakis K.A.;
RT "Bridging the gap between plant and mammalian polyamine catabolism: a novel
RT peroxisomal polyamine oxidase responsible for a full back-conversion
RT pathway in Arabidopsis thaliana.";
RL Plant Physiol. 147:1845-1857(2008).
RN [8]
RP FUNCTION.
RX PubMed=20532512; DOI=10.1007/s00299-010-0881-1;
RA Takahashi Y., Cong R., Sagor G.H., Niitsu M., Berberich T., Kusano T.;
RT "Characterization of five polyamine oxidase isoforms in Arabidopsis
RT thaliana.";
RL Plant Cell Rep. 29:955-965(2010).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21081665; DOI=10.1093/jxb/erq341;
RA Fincato P., Moschou P.N., Spedaletti V., Tavazza R., Angelini R.,
RA Federico R., Roubelakis-Angelakis K.A., Tavladoraki P.;
RT "Functional diversity inside the Arabidopsis polyamine oxidase gene
RT family.";
RL J. Exp. Bot. 62:1155-1168(2011).
RN [10]
RP FUNCTION.
RX PubMed=26925084; DOI=10.3389/fpls.2016.00173;
RA Sequera-Mutiozabal M.I., Erban A., Kopka J., Atanasov K.E., Bastida J.,
RA Fotopoulos V., Alcazar R., Tiburcio A.F.;
RT "Global metabolic profiling of Arabidopsis polyamine oxidase 4 (AtPAO4)
RT loss-of-function mutants exhibiting delayed dark-induced senescence.";
RL Front. Plant Sci. 7:173-173(2016).
CC -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion
CC (PubMed:18703589, PubMed:20532512, PubMed:21081665, PubMed:26925084).
CC Catalyzes the oxidation of the secondary amino group of polyamines,
CC such as spermine and spermidine (PubMed:18703589, PubMed:20532512,
CC PubMed:21081665, PubMed:26925084). Substrate preference is spermine >
CC spermidine (PubMed:18703589, PubMed:21081665). No activity detected
CC when putrescine or N(1)-acetylspermine are used as substrates
CC (PubMed:18703589). Plays an important role in the regulation of
CC polyamine intracellular concentration (Probable).
CC {ECO:0000269|PubMed:18703589, ECO:0000269|PubMed:20532512,
CC ECO:0000269|PubMed:21081665, ECO:0000269|PubMed:26925084,
CC ECO:0000305|PubMed:21081665}.
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; EC=1.5.3.16;
CC Evidence={ECO:0000269|PubMed:18703589};
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:18703589};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:18703589};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:18703589};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 mM for spermine {ECO:0000269|PubMed:18703589};
CC KM=0.047 mM for spermine {ECO:0000269|PubMed:21081665};
CC KM=0.137 mM for spermidine {ECO:0000269|PubMed:21081665};
CC pH dependence:
CC Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:18703589};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305}.
CC -!- PATHWAY: Amine and polyamine degradation; spermidine degradation.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:18703589}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, flowers and greening
CC cotelydons. Lower expression in other tissues.
CC {ECO:0000269|PubMed:18703589}.
CC -!- INDUCTION: By abscisic acid, salicylic acid, wounding and flagellin 22,
CC a pathogen elicitor. {ECO:0000269|PubMed:18583528}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18703589}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23834.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF364953; AAO85405.1; -; mRNA.
DR EMBL; AC007234; AAF23834.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34430.1; -; Genomic_DNA.
DR EMBL; AF370508; AAK43885.1; -; mRNA.
DR EMBL; BT000353; AAN15672.1; -; mRNA.
DR PIR; D96682; D96682.
DR RefSeq; NP_176759.1; NM_105256.4.
DR AlphaFoldDB; Q8H191; -.
DR SMR; Q8H191; -.
DR STRING; 3702.AT1G65840.1; -.
DR PaxDb; Q8H191; -.
DR PRIDE; Q8H191; -.
DR ProteomicsDB; 248658; -.
DR EnsemblPlants; AT1G65840.1; AT1G65840.1; AT1G65840.
DR GeneID; 842894; -.
DR Gramene; AT1G65840.1; AT1G65840.1; AT1G65840.
DR KEGG; ath:AT1G65840; -.
DR Araport; AT1G65840; -.
DR TAIR; locus:2018571; AT1G65840.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_10_0_1; -.
DR InParanoid; Q8H191; -.
DR OMA; GGQWIGH; -.
DR OrthoDB; 1034142at2759; -.
DR PhylomeDB; Q8H191; -.
DR BioCyc; ARA:AT1G65840-MON; -.
DR BioCyc; MetaCyc:AT1G65840-MON; -.
DR BRENDA; 1.5.3.16; 399.
DR UniPathway; UPA00211; -.
DR UniPathway; UPA00250; -.
DR PRO; PR:Q8H191; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H191; baseline and differential.
DR Genevisible; Q8H191; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0052895; F:N1-acetylspermine:oxygen oxidoreductase (N1-acetylspermidine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052894; F:norspermine:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase activity; IDA:TAIR.
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; IEA:UniProtKB-EC.
DR GO; GO:0006598; P:polyamine catabolic process; IDA:TAIR.
DR GO; GO:0046203; P:spermidine catabolic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..497
FT /note="Probable polyamine oxidase 4"
FT /id="PRO_0000352510"
FT MOTIF 495..497
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 247
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT BINDING 435
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O64411"
FT CONFLICT 283
FT /note="K -> R (in Ref. 4; AAK43885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 54931 MW; 69CEE30B841B022C CRC64;
MDKKKNSFPD NLPEGTISEL MQKQNNVQPS VIVIGSGISG LAAARNLSEA SFKVTVLESR
DRIGGRIHTD YSFGCPVDMG ASWLHGVSDE NPLAPIIRRL GLTLYRTSGD DSILYDHDLE
SYGLFDMHGN KIPPQLVTKV GDAFKRILEE TEKIRDETAN DMSVLQGISI VLDRNPELRQ
EGMAYEVLQW YLCRMEAWFA VDANLISLKC WDQDECLSGG HGLMVQGYEP VIRTIAKDLD
IRLNHRVTKV VRTSNNKVIV AVEGGTNFVA DAVIITVPIG VLKANLIQFE PELPQWKTSA
ISGLGVGNEN KIALRFDRAF WPNVEFLGMV APTSYACGYF LNLHKATGHP VLVYMAAGNL
AQDLEKLSDE ATANFVMLQL KKMFPDAPDP AQYLVTRWGT DPNTLGCYAY DVVGMPEDLY
PRLGEPVDNI FFGGEAVNVE HQGSAHGAFL AGVSASQNCQ RYIFERLGAW EKLKLVSLMG
NSDILETATV PLQISRM
