AMO2_ARATH
ID AMO2_ARATH Reviewed; 662 AA.
AC P0DO00; Q9C6V7;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Primary amine oxidase 2;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P12807};
DE AltName: Full=Amine oxidase [copper-containing] 2;
DE Flags: Precursor;
GN OrderedLocusNames=At1g31672 {ECO:0000305};
GN ORFNames=F27M3.13 {ECO:0000312|EMBL:AAG60154.1};
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).
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:0000250|UniProtKB:P12807};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q43077};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q43077};
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 -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000250|UniProtKB:Q43077};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000250|UniProtKB:Q43077};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q43077}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:Q43077}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG60154.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g31670 has been split into 2 genes: At1g31670 and At1g31672.; Evidence={ECO:0000305};
CC Sequence=AEE31382.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g31670 has been split into 2 genes: At1g31670 and At1g31672.; Evidence={ECO:0000305};
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DR EMBL; AC074360; AAG60154.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31382.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P0DO00; -.
DR SMR; P0DO00; -.
DR STRING; 3702.AT1G31670.1; -.
DR PRIDE; P0DO00; -.
DR ProteomicsDB; 244986; -.
DR EnsemblPlants; AT1G31670.1; AT1G31670.1; AT1G31670.
DR Gramene; AT1G31670.1; AT1G31670.1; AT1G31670.
DR Araport; AT1G31672; -.
DR eggNOG; KOG1186; Eukaryota.
DR PRO; PR:P0DO00; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P0DO00; baseline and differential.
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; 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 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.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 3: Inferred from homology;
KW Copper; Disulfide bond; Glycoprotein; Manganese; Metal-binding;
KW Oxidoreductase; Reference proteome; Signal; TPQ.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..662
FT /note="Primary amine oxidase 2"
FT /id="PRO_5009973652"
FT ACT_SITE 323
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 408
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 321..332
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 405..410
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 464
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 466
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 473
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 475
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 602
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 603
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 613
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT MOD_RES 408
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT DISULFID 342..368
FT /evidence="ECO:0000250|UniProtKB:Q43077"
SQ SEQUENCE 662 AA; 75363 MW; C76FCE69D52BF85F CRC64;
MSQLLLFTIL VFSSVFVIGS LSFIPPPHPF DPLTEIELNL VRNIINERYP IGLEHRFTFQ
YVGLNEPDKS LVLSWVSSQY HNVKSPPRQA FVIARDHGKT REIVVDFASQ AIVSEKIHVG
NGYPMLTIDE QQATSELVLK FKPFRDSIRR RGLNVSEVVV TTSTMGWFGE AKPERLIKKR
PFYLNGSVNT YLRPIEGMTI IVNLDQMKVT KFRDRFTSPL PNAKGTEFRI SKLKPPFGPS
LQNAVLFQSE GPGFKIDGHT NRWANWEFHM SFDVRAGLVI SLASIFDMDV NKYRQVLYKG
HLSEIFVPYM DPSEDWYFRT FFDCGEFGCG QYAVSLEPYT DCPGNAAFMD GVFASQDGTP
IKITNVMCIF EKYAGDIMWR HTEIEIPGLK VRPDVSLVVR MVTTVGNYDY IVDYEFKPSG
SIKIGVGLTG VLEVKPVKYV NTSEIKEDDI HGTIVADNTI GVNHDHFVTY RLDLDIDGTD
NSFVRSELVT KRTPKSVNTP RKSYWTTKRL KAEELLVVNP SRKTKHGNEV GYRLLHGPAS
EGPLLAQDDY PQIRAAFTNY NVWITPYNNT EVWASGLYAD RSQGDDTLAV WSQRNRKIEK
TDIVMWYTVG FHHVPCQEDF PTMPTLFGGF ELRPTNFFEQ NPDLKTKPIK LNTTPTCTAR
ND
