ID   CAOA2_ARATH             Reviewed;         677 AA.
AC   F4IAX0; Q9C6V8; Q9C6V9;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Amine oxidase [copper-containing] alpha 2, peroxisomal {ECO:0000303|PubMed:31862580};
DE            Short=AtCuAO8 {ECO:0000303|PubMed:28383668};
DE            Short=AtCuAOalpha2 {ECO:0000303|PubMed:31862580};
DE            EC=1.4.3.21 {ECO:0000269|PubMed:28383668};
GN   Name=CuAOalpha2 {ECO:0000303|PubMed:31862580};
GN   Synonyms=CuAO8 {ECO:0000303|PubMed:28383668};
GN   OrderedLocusNames=At1g31690 {ECO:0000312|Araport:AT1G31690};
GN   ORFNames=F27M3.11 {ECO:0000312|EMBL:AAG60148.1}, F27M3.12
GN   {ECO:0000312|EMBL:AAG60151.1};
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=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   [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   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=cv. Columbia;
RX   PubMed=28383668; DOI=10.1093/jxb/erx105;
RA   Gross F., Rudolf E.-E., Thiele B., Durner J., Astier J.;
RT   "Copper amine oxidase 8 regulates arginine-dependent nitric oxide
RT   production in Arabidopsis thaliana.";
RL   J. Exp. Bot. 68:2149-2162(2017).
RN   [4]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY JASMONATE; ABSCISIC
RP   ACID; SALICYLIC ACID; DEHYDRATION RECOVERY; WOUNDING; PUTRESCINE AND AUXIN,
RP   GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
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: Copper amine oxidase that can use putrescine and spermidine
CC       as substrates (PubMed:28383668). Involved in putrescine catabolism in
CC       peroxisomes in response to salt stress (PubMed:28383668). Regulates
CC       arginine-dependent nitric oxide (NO) production, a key signaling
CC       molecule regulating a wide range of physiological processes including
CC       responses to salt stress, by influencing arginine bioavailability
CC       (PubMed:28383668). Modulates primary root growth (PubMed:28383668).
CC       {ECO:0000269|PubMed:28383668}.
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:28383668};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154;
CC         Evidence={ECO:0000269|PubMed:28383668};
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   -!- PATHWAY: Amine and polyamine degradation; putrescine degradation.
CC       {ECO:0000269|PubMed:28383668}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A1S4BDC4}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:F4IAX1}.
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in leaves.
CC       {ECO:0000269|PubMed:31862580}.
CC   -!- DEVELOPMENTAL STAGE: In young seedlings, first observed in hydathodes
CC       and borders of new emerging cotyledons and in leaf primordia
CC       (PubMed:31862580). Accumulates in expanding leaves (PubMed:31862580).
CC       {ECO:0000269|PubMed:31862580}.
CC   -!- INDUCTION: Induced transiently by auxin (IAA) (PubMed:31862580).
CC       Accumulates during dehydration recovery, wounding and treatment with
CC       putrescine (Put) and jasmonic acid (MeJA) (PubMed:31862580). Repressed
CC       by abscisic acid (ABA) and salicylic acid (SA) (PubMed:31862580).
CC       {ECO:0000269|PubMed:31862580}.
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC       a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
CC   -!- DISRUPTION PHENOTYPE: Decreased nitric oxide (NO) production in
CC       seedlings after elicitor treatment with 2,6-dichloroisonicotinic acid
CC       (INA) in root tips and salt stress associated with a reduced arginine
CC       availability but with a normal nitrate reductase activity in plants
CC       (PubMed:28383668). Reduced primary root length (PubMed:28383668).
CC       {ECO:0000269|PubMed:28383668}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG60148.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG60151.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC074360; AAG60148.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC074360; AAG60151.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31383.1; -; Genomic_DNA.
DR   RefSeq; NP_174450.2; NM_102904.3.
DR   AlphaFoldDB; F4IAX0; -.
DR   SMR; F4IAX0; -.
DR   STRING; 3702.F4IAX0; -.
DR   PaxDb; 3702-AT1G31690-1; -.
DR   ProteomicsDB; 197390; -.
DR   EnsemblPlants; AT1G31690.1; AT1G31690.1; AT1G31690.
DR   GeneID; 840056; -.
DR   Gramene; AT1G31690.1; AT1G31690.1; AT1G31690.
DR   KEGG; ath:AT1G31690; -.
DR   Araport; AT1G31690; -.
DR   TAIR; AT1G31690; CUAOALPHA2.
DR   eggNOG; KOG1186; Eukaryota.
DR   HOGENOM; CLU_011500_5_4_1; -.
DR   InParanoid; F4IAX0; -.
DR   OMA; QHAVWVT; -.
DR   OrthoDB; 5490352at2759; -.
DR   BioCyc; ARA:AT1G31690-MONOMER; -.
DR   BRENDA; 1.4.3.21; 399.
DR   UniPathway; UPA00188; -.
DR   PRO; PR:F4IAX0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4IAX0; baseline and differential.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR   GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
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:0090465; P:intracellular arginine homeostasis; IMP:UniProtKB.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0080022; P:primary root development; IMP:UniProtKB.
DR   GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR   GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR   GO; GO:1904585; P:response to putrescine; IEP:UniProtKB.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR   GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR   GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR   Gene3D; 3.10.450.40; -; 2.
DR   Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 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; IPR015800; Cu_amine_oxidase_N2.
DR   InterPro; IPR015802; Cu_amine_oxidase_N3.
DR   PANTHER; PTHR10638:SF87; AMINE OXIDASE-RELATED; 1.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   Pfam; PF02728; Cu_amine_oxidN3; 1.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE   1: Evidence at protein level;
KW   Copper; Disulfide bond; Manganese; Metal-binding; Oxidoreductase;
KW   Peroxisome; Reference proteome; TPQ.
FT   CHAIN           1..677
FT                   /note="Amine oxidase [copper-containing] alpha 2,
FT                   peroxisomal"
FT                   /id="PRO_5003309597"
FT   ACT_SITE        322
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   ACT_SITE        410
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         320..331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         407..412
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P46883"
FT   BINDING         466
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         468
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         477
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         617
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         618
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         628
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   MOD_RES         410
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   DISULFID        341..367
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
SQ   SEQUENCE   677 AA;  76674 MW;  A4A45980995368DC CRC64;
     MAQVHLTIFI FSSIFVISSS SFIPPPHPFD PLTETELKLV RNIINKSYPI GHNHKFTFQY
     VGLNEPEKSL VLSWHSSPDR NVKPPPRQAF VIARDKGMSR EIVIDFSTRA IVSNKIHVGN
     GNPMLTIDEQ QAATAVVQKY KPFCDSIIKR GLNLSEVVVT SSTMGWFGET KTKRFIRTIP
     FYLNGSVNTY LRPIEGMTII VNLDQMKVTG FKDRFTGPMP KANGREYRIS KLKPPFGPSL
     RSAVVFQPDG PGFKIDGHVV RWANWEFHMS FDVRAGLVIS LASIFDMDMN RYRQVLYKGH
     LSEMFVPYMD PNDDWYFISY LDCGEFGCGQ TAVSLEPYTD CPPNAAFMDG IFPGQDGTPT
     KISNVMCIFE KYAGDIMWRH TEAEVPGLKI TEVRPDVSLV ARMVTTVGNY DYIIEYEFKP
     SGSIKMGVGL TGVLEVKPVE YVHTSEIKED DIYGTIVADN TVGVNHDHFV TFRLDLDIDG
     TENSFVRTEL VTKRTPKSVN TPRKSYWTTK RNTAKTEADA RVKLGLRAEE LVVVNPTKKT
     KHGNEVGYRL LPGPASSPLL VQDDYPQIRA AFTNYNVWIT PYNKSEVWAS GLYADRSQGD
     DTLAVWSQRD REIENKDIVM WYTVGFHHVP CQEDFPTMPT MFGGFELRPT NFFEQNPVLK
     AKPFNLTTIP KCTTKNE
//