CUAOZ_ARATH
ID CUAOZ_ARATH Reviewed; 776 AA.
AC Q8L866; Q56W61; Q9SLB1;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Amine oxidase [copper-containing] zeta, peroxisomal {ECO:0000303|PubMed:31862580};
DE Short=AtCuAO1 {ECO:0000303|PubMed:24287136};
DE Short=AtCuAO3 {ECO:0000303|PubMed:23915037};
DE Short=AtCuAOzeta {ECO:0000303|PubMed:31862580};
DE Short=Copper amine oxidase 3 {ECO:0000303|PubMed:23915037};
DE EC=1.4.3.21 {ECO:0000269|PubMed:23915037, ECO:0000269|PubMed:24287136};
GN Name=CuAOzeta {ECO:0000303|PubMed:31862580};
GN Synonyms=CuAO1 {ECO:0000303|PubMed:24287136},
GN CuAO3 {ECO:0000303|PubMed:23915037};
GN OrderedLocusNames=At2g42490 {ECO:0000312|Araport:AT2G42490};
GN ORFNames=F14N22.1 {ECO:0000312|EMBL:AAM15387.1},
GN MHK10.21 {ECO:0000312|EMBL:AAD23730.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-776.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY SALICYLIC ACID; JASMONATE;
RP WOUNDING; FLAGELLIN AND ABCISIC ACID, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=23915037; DOI=10.1186/1471-2229-13-109;
RA Planas-Portell J., Gallart M., Tiburcio A.F., Altabella T.;
RT "Copper-containing amine oxidases contribute to terminal polyamine
RT oxidation in peroxisomes and apoplast of Arabidopsis thaliana.";
RL BMC Plant Biol. 13:109-109(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=24287136; DOI=10.1093/pcp/pct179;
RA Naconsie M., Kato K., Shoji T., Hashimoto T.;
RT "Molecular evolution of N-methylputrescine oxidase in tobacco.";
RL Plant Cell Physiol. 55:436-444(2014).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=31862580; DOI=10.1016/j.plaphy.2019.11.037;
RA Fraudentali I., Ghuge S.A., Carucci A., Tavladoraki P., Angelini R.,
RA Rodrigues-Pousada R.A., Cona A.;
RT "Developmental, hormone- and stress-modulated expression profiles of four
RT members of the Arabidopsis copper-amine oxidase gene family.";
RL Plant Physiol. Biochem. 147:141-160(2020).
CC -!- FUNCTION: Involved in putrescine catabolism in peroxisomes
CC (PubMed:24287136). Copper amine oxidase that can use putrescine and
CC spermidine as substrates (PubMed:23915037).
CC {ECO:0000269|PubMed:23915037, ECO:0000269|PubMed:24287136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000269|PubMed:23915037, ECO:0000269|PubMed:24287136};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154;
CC Evidence={ECO:0000269|PubMed:23915037, ECO:0000269|PubMed:24287136};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P12807};
CC Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc
CC ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807,
CC ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000250|UniProtKB:P46883};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=208 uM for putrescine {ECO:0000269|PubMed:24287136};
CC KM=896 uM for N-methylputrescine {ECO:0000269|PubMed:24287136};
CC KM=1855 uM for cadaverine {ECO:0000269|PubMed:24287136};
CC Vmax=690 pmol/sec/mg enzyme with putrescine as substrate
CC {ECO:0000269|PubMed:24287136};
CC Vmax=1445 pmol/sec/mg enzyme with N-methylputrescine as substrate
CC {ECO:0000269|PubMed:24287136};
CC Vmax=2715 pmol/sec/mg enzyme with cadaverine as substrate
CC {ECO:0000269|PubMed:24287136};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation.
CC {ECO:0000269|PubMed:23915037, ECO:0000269|PubMed:24287136}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A1S4BDC4}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:23915037}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, and, at lower levels,
CC in stems and leaves. {ECO:0000269|PubMed:23915037}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during aging.
CC {ECO:0000269|PubMed:23915037}.
CC -!- INDUCTION: Induced by salicylic acid (SA), jasmonic acid (MeJA),
CC wounding, flagellin 22 (fgl22) and abcisic acid (ABA).
CC {ECO:0000269|PubMed:23915037}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD23730.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15387.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD95322.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC005956; AAD23730.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007087; AAM15387.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10126.1; -; Genomic_DNA.
DR EMBL; AY120717; AAM53275.1; -; mRNA.
DR EMBL; BT000029; AAN15348.1; -; mRNA.
DR EMBL; AK222186; BAD95322.1; ALT_INIT; mRNA.
DR PIR; E84854; E84854.
DR RefSeq; NP_181777.2; NM_129810.5.
DR SMR; Q8L866; -.
DR IntAct; Q8L866; 8.
DR STRING; 3702.AT2G42490.1; -.
DR PRIDE; Q8L866; -.
DR ProteomicsDB; 190038; -.
DR EnsemblPlants; AT2G42490.1; AT2G42490.1; AT2G42490.
DR GeneID; 818849; -.
DR Gramene; AT2G42490.1; AT2G42490.1; AT2G42490.
DR KEGG; ath:AT2G42490; -.
DR Araport; AT2G42490; -.
DR TAIR; locus:2041589; AT2G42490.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_2_1; -.
DR OMA; NEMTVPY; -.
DR OrthoDB; 1320015at2759; -.
DR BRENDA; 1.4.3.21; 399.
DR UniPathway; UPA00188; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L866; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0010311; P:lateral root formation; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
PE 1: Evidence at protein level;
KW Copper; Disulfide bond; Manganese; Metal-binding; Oxidoreductase;
KW Peroxisome; Reference proteome; TPQ.
FT CHAIN 1..776
FT /note="Amine oxidase [copper-containing] zeta, peroxisomal"
FT /id="PRO_0000455785"
FT ACT_SITE 412
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 496
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 410..421
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 493..498
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 546
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 548
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 555
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 701
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 712
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT SITE 774..776
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 496
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT DISULFID 431..457
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT CONFLICT 601
FT /note="V -> L (in Ref. 4; BAD95322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 776 AA; 86691 MW; 61C4EBFE38985326 CRC64;
MASASKKTSA CPHHGGSLPP PKLVSAAPDT VAVWSDADDQ RASKVSLESV IRPVDSFPDN
TAKKPANKGI SVMPRTETKH PLDPLSAAEI SVAVATVRAA GANPEVRDGM RFIEVASVEP
DKQVVALADA YFFPPFQPSL LPRTKSGPVI PMKLPPRRAR LVVYNQKSNE TSVWIVALSE
VHAVTRGGHH RGRVVSSQVI PDVQPPMDAA EYAECEAIVK DFPPFIEAMK RRGIEDMDLV
MVDPWCVGYH SEADAPSRRL AKPLIYCRTD SDSPMENGYA RPVEGIYVLV DMQNMVVIEF
EDRKFVPLPP PDPLRNYTPG ESRGGVDRSD VKPLQIIQPE GPSFRVRGYF VEWQKWNFRI
GFTPREGLVI HSVAYVDGSR GRRPVAHRLS FVEMVVPYGD PNEPHYRKNA FDAGEDGLGK
NAHSLKKGCD CLGSIKYFDA HFTNFTGGVE TIENCVCLHE EDHGILWKHQ DWRTGLAEVR
RSRRLTVSFL CTVANYEYGF YWHFYQDGKI EAEVKLTGIL SLGALQPGET RKYGTTIAPG
LYAPVHQHFF IARMDMSVDC KPAEAFNQVV EVNVRVDERG ENNVHNNAFY AEEKLLKSEA
VAMRDCDPLS ARHWIVRNTR TVNRTGQLTG YKLVPGSNCL PLARPEAKFL RRAAFLKHNL
WVTRYAPDEK FPGGEFPNQN PRAGEGLATW VKQNRSLEES DVVLWYVFGI THVPRLEDWP
VMPVEHIGFT LMPHGFFNCS PAVDVPPNPC ELETKESEVK EVVAPKALQT GLLSKL
