AO1_ARATH
ID AO1_ARATH Reviewed; 650 AA.
AC O23349; O48552;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Primary amine oxidase 1 {ECO:0000303|PubMed:9681017};
DE Short=AtAO1 {ECO:0000303|PubMed:9681017};
DE EC=1.4.3.21 {ECO:0000269|PubMed:9681017};
DE Flags: Precursor;
GN Name=AO1 {ECO:0000303|PubMed:9681017};
GN OrderedLocusNames=At4g14940 {ECO:0000312|Araport:AT4G14940};
GN ORFNames=dl3510w {ECO:0000312|EMBL:CAB10273.1},
GN FCAALL.145 {ECO:0000312|EMBL:CAB78536.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP DEVELOPMENTAL STAGE, AND ACTIVITY REGULATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9681017; DOI=10.1046/j.1365-313x.1998.00080.x;
RA Moeller S.G., McPherson M.J.;
RT "Developmental expression and biochemical analysis of the Arabidopsis atao1
RT gene encoding an H2O2-generating diamine oxidase.";
RL Plant J. 13:781-791(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, INDUCTION BY JASMONIC
RP ACID, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25883242; DOI=10.1104/pp.15.00121;
RA Ghuge S.A., Carucci A., Rodrigues-Pousada R.A., Tisi A., Franchi S.,
RA Tavladoraki P., Angelini R., Cona A.;
RT "The apoplastic copper AMINE OXIDASE1 mediates jasmonic acid-induced
RT protoxylem differentiation in Arabidopsis roots.";
RL Plant Physiol. 168:690-707(2015).
CC -!- FUNCTION: Oxidizes preferentially the aliphatic diamine putrescine with
CC production of the corresponding aldehyde, ammonia and hydrogen
CC peroxide. May be involved in the regulation of developmental programmed
CC cell death (PCD) in both vascular tissue and the root cap
CC (PubMed:9681017). Required for jasmonic acid-(MeJA) mediated early
CC protoxylem differentiation associated with putrescine levels reduction
CC and H(2)O(2) accumulation in roots (PubMed:25883242).
CC {ECO:0000269|PubMed:25883242, ECO:0000269|PubMed:9681017}.
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:9681017};
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 -!- 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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q43077};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077};
CC -!- ACTIVITY REGULATION: Repressed by semi-carbazide, a specific and
CC irreversible inhibitor of copper amine oxidases.
CC {ECO:0000269|PubMed:9681017}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46883}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:H2A0M3}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissues at the
CC division/differentiation transition zone.
CC {ECO:0000269|PubMed:25883242}.
CC -!- DEVELOPMENTAL STAGE: Levels peak 3-4 days after germination. Expressed
CC following temporally and spatially discrete patterns of gene expression
CC in lateral root cap cells, vascular tissue of roots, developing leaves,
CC the hypocotyl, and in the style/stigmatal tissue (PubMed:9681017).
CC Expressed at the early stages of vascular tissue differentiation in
CC roots; strong accumulation in the protoxylem at the transition,
CC elongation, and maturation zones (PubMed:25883242). Accumulates in
CC developing tracheary elements before lignification. Present in cells
CC destined to undergo programmed cell death (PCD) in both vascular tissue
CC and the root cap. In flowers, restricted spatial and temporal
CC distribution; at stage 11-13, after papillae formation, accumulates in
CC tracheary elements of style and stigmate (PubMed:9681017).
CC {ECO:0000269|PubMed:25883242, ECO:0000269|PubMed:9681017}.
CC -!- INDUCTION: Induced by jasmonic acid (MeJA) in vascular tissues,
CC especially at the transition and elongation zones.
CC {ECO:0000269|PubMed:25883242}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
CC -!- DISRUPTION PHENOTYPE: Impaired sensitivity to jasmonic acid (MeJA).
CC {ECO:0000269|PubMed:25883242}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB87690.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF034579; AAB87690.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z97337; CAB10273.1; -; Genomic_DNA.
DR EMBL; AL161540; CAB78536.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83525.1; -; Genomic_DNA.
DR PIR; G71412; G71412.
DR RefSeq; NP_193230.1; NM_117580.2.
DR AlphaFoldDB; O23349; -.
DR SMR; O23349; -.
DR STRING; 3702.AT4G14940.1; -.
DR iPTMnet; O23349; -.
DR PaxDb; O23349; -.
DR PRIDE; O23349; -.
DR ProteomicsDB; 245008; -.
DR EnsemblPlants; AT4G14940.1; AT4G14940.1; AT4G14940.
DR GeneID; 827152; -.
DR Gramene; AT4G14940.1; AT4G14940.1; AT4G14940.
DR KEGG; ath:AT4G14940; -.
DR Araport; AT4G14940; -.
DR TAIR; locus:2129520; AT4G14940.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_5_4_1; -.
DR InParanoid; O23349; -.
DR OMA; SHAVWVT; -.
DR OrthoDB; 1320015at2759; -.
DR PhylomeDB; O23349; -.
DR BioCyc; MetaCyc:AT4G14940-MON; -.
DR PRO; PR:O23349; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23349; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
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; IDA:TAIR.
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:0009867; P:jasmonic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0090059; P:protoxylem development; IMP:UniProtKB.
DR GO; GO:0043067; P:regulation of programmed cell death; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; 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; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 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; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Copper; Disulfide bond; Glycoprotein;
KW Jasmonic acid signaling pathway; Manganese; Metal-binding; Oxidoreductase;
KW Reference proteome; Secreted; Signal; TPQ.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..650
FT /note="Primary amine oxidase 1"
FT /id="PRO_5008172703"
FT ACT_SITE 310
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 398
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 308..319
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 395..400
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 453
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 455
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 462
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 464
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 607
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 608
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 618
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MOD_RES 398
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 155..176
FT /evidence="ECO:0000250"
FT DISULFID 329..355
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CONFLICT 103
FT /note="T -> I (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="V -> I (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="I -> V (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..217
FT /note="IPD -> LPE (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..233
FT /note="TKHRPFPFF -> KKHKPFPFS (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="L -> F (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="E -> A (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="N -> S (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="D -> E (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="L -> Q (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="E -> D (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="D -> E (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="Q -> P (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="L -> I (in Ref. 1; AAB87690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 73783 MW; 28741CEB3A43FF5D CRC64;
MNTSILAILF LIQCVFTLGL HFHPLDPLTP QEINKTSFIV KKSHLGNLKD LTFHYLDLEE
PNKSHVLQWL SPNPSKKPPP PRRRSFVVVR AGGQTYELII DLTTSKIASS RIYTGHGFPS
FTFIELFKAS KLPLTYPPFK KSILDRSLNI SEVSCIPFTV GWYGETTTRR ELKASCFYRD
GSVNVFTRPI EGITVTIDVD SMQVIKYSDR FRKPIPDKEG NDFRTKHRPF PFFCNVSDTG
FKILGNRVKW ANWKFHVGFT ARAGVTISTA SVLDPRTKRF RRVMYRGHVS ETFVPYMDPT
YEWYYRTFMD IGEFGFGRSA VNLQPLIDCP QNAAFLDGHV AGPDGTAQKM TNVMCVFEKN
GYGASFRHTE INVPGQVITS GEAEISLVVR MVATLGNYDY IVDWEFKKNG AIRVGVDLTG
VLEVKATSYT SNDQITENVY GTLVAKNTIA VNHDHYLTYY LDLDVDGNGN SLVKAKLKTV
RVTEVNKTSS RRKSYWTVVK ETAKTEADGR VRLGSDPVEL LIVNPNKKTK IGNTVGYRLI
PEHLQATSLL TDDDYPELRA GYTKYPVWVT AYDRSERWAG GFYSDRSRGD DGLAVWSSRN
REIENKDIVM WYNVGFHHIP YQEDFPVMPT LHGGFTLRPS NFFDNDPLIG
