AMO_PEA
ID AMO_PEA Reviewed; 674 AA.
AC Q43077;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Primary amine oxidase;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P12807};
DE AltName: Full=Amine oxidase [copper-containing];
DE Flags: Precursor;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tipping A.J., McPherson M.J.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 31-672 IN COMPLEX WITH COPPER AND
RP MANGANESE, TOPAQUINONE AT TYR-412, GLYCOSYLATION AT ASN-156, DISULFIDE
RP BOND, AND SUBUNIT.
RC TISSUE=Seedling;
RX PubMed=8805580; DOI=10.1016/s0969-2126(96)00101-3;
RA Kumar V., Dooley D.M., Freeman H.C., Guss J.M., Harvey I., McGuirl M.A.,
RA Wilce M.C., Zubak V.M.;
RT "Crystal structure of a eukaryotic (pea seedling) copper-containing amine
RT oxidase at 2.2-A resolution.";
RL Structure 4:943-955(1996).
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:0000269|PubMed:8805580};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:8805580};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:8805580};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:8805580};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000269|PubMed:8805580};
CC Note=Contains 1 topaquinone per subunit. {ECO:0000269|PubMed:8805580};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8805580}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000269|PubMed:8805580}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR EMBL; L39931; AAA62490.1; -; Genomic_DNA.
DR PIR; A57327; C44239.
DR PDB; 1KSI; X-ray; 2.20 A; A/B=31-672.
DR PDB; 1W2Z; X-ray; 2.24 A; A/B/C/D=26-674.
DR PDBsum; 1KSI; -.
DR PDBsum; 1W2Z; -.
DR AlphaFoldDB; Q43077; -.
DR SMR; Q43077; -.
DR BindingDB; Q43077; -.
DR ChEMBL; CHEMBL5534; -.
DR iPTMnet; Q43077; -.
DR KEGG; ag:AAA62490; -.
DR BRENDA; 1.4.3.21; 4872.
DR SABIO-RK; Q43077; -.
DR EvolutionaryTrace; Q43077; -.
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; IEA:InterPro.
DR GO; GO:0052597; F:diamine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase 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:0009308; P:amine metabolic process; IEA:InterPro.
DR GO; GO:0097185; P:cellular response to azide; IDA: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 3D-structure; Copper; Disulfide bond; Glycoprotein; Manganese;
KW Metal-binding; Oxidoreductase; Signal; TPQ.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..674
FT /note="Primary amine oxidase"
FT /id="PRO_0000035680"
FT REGION 226..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 412
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 323..334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 409..414
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 467
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT BINDING 469
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT BINDING 476
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT BINDING 477
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT BINDING 478
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT BINDING 617
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT BINDING 618
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT BINDING 628
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT MOD_RES 412
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 162..183
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT DISULFID 344..370
FT /evidence="ECO:0000269|PubMed:8805580,
FT ECO:0007744|PDB:1KSI"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:1KSI"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:1KSI"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1KSI"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1W2Z"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:1KSI"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 279..289
FT /evidence="ECO:0007829|PDB:1KSI"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 294..311
FT /evidence="ECO:0007829|PDB:1KSI"
FT TURN 316..320
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:1KSI"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:1KSI"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 362..384
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 392..409
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 467..477
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 484..495
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:1W2Z"
FT STRAND 504..513
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 529..539
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 565..569
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 603..606
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 607..609
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 618..628
FT /evidence="ECO:0007829|PDB:1KSI"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 646..651
FT /evidence="ECO:0007829|PDB:1KSI"
FT STRAND 653..655
FT /evidence="ECO:0007829|PDB:1KSI"
FT TURN 657..660
FT /evidence="ECO:0007829|PDB:1KSI"
SQ SEQUENCE 674 AA; 76358 MW; 30735390071DD18E CRC64;
MASTTTMRLA LFSVLTLLSF HAVVSVTPLH VQHPLDPLTK EEFLAVQTIV QNKYPISNNR
LAFHYIGLDD PEKDHVLRYE THPTLVSIPR KIFVVAIINS QTHEILINLR IRSIVSDNIH
NGYGFPILSV DEQSLAIKLP LKYPPFIDSV KKRGLNLSEI VCSSFTMGWF GEEKNVRTVR
LDCFMKESTV NIYVRPITGI TIVADLDLMK IVEYHDRDIE AVPTAENTEY QVSKQSPPFG
PKQHSLTSHQ PQGPGFQING HSVSWANWKF HIGFDVRAGI VISLASIYDL EKHKSRRVLY
KGYISELFVP YQDPTEEFYF KTFFDSGEFG FGLSTVSLIP NRDCPPHAQF IDTYVHSANG
TPILLKNAIC VFEQYGNIMW RHTENGIPNE SIEESRTEVN LIVRTIVTVG NYDNVIDWEF
KASGSIKPSI ALSGILEIKG TNIKHKDEIK EDLHGKLVSA NSIGIYHDHF YIYYLDFDID
GTHNSFEKTS LKTVRIKDGS SKRKSYWTTE TQTAKTESDA KITIGLAPAE LVVVNPNIKT
AVGNEVGYRL IPAIPAHPLL TEDDYPQIRG AFTNYNVWVT AYNRTEKWAG GLYVDHSRGD
DTLAVWTKQN REIVNKDIVM WHVVGIHHVP AQEDFPIMPL LSTSFELRPT NFFERNPVLK
TLSPRDVAWP GCSN
