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Primary amine oxidase (EC 1.4.3.21) (Amine oxidase [copper-containing])

 AMO_PEA                 Reviewed;         674 AA.
Q43077;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 98.
RecName: Full=Primary amine oxidase;
EC=1.4.3.21 {ECO:0000250|UniProtKB:P12807};
AltName: Full=Amine oxidase [copper-containing];
Flags: Precursor;
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tipping A.J., McPherson M.J.;
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[2]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 31-672 IN COMPLEX WITH
COPPER AND MANGANESE, TOPAQUINONE AT TYR-412, GLYCOSYLATION AT
ASN-156, DISULFIDE BOND, AND SUBUNIT.
TISSUE=Seedling;
PubMed=8805580; DOI=10.1016/S0969-2126(96)00101-3;
Kumar V., Dooley D.M., Freeman H.C., Guss J.M., Harvey I.,
McGuirl M.A., Wilce M.C., Zubak V.M.;
"Crystal structure of a eukaryotic (pea seedling) copper-containing
amine oxidase at 2.2-A resolution.";
Structure 4:943-955(1996).
-!- CATALYTIC ACTIVITY: RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) +
H(2)O(2). {ECO:0000250|UniProtKB:P12807}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000269|PubMed:8805580};
Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:8805580};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:8805580};
Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:8805580};
-!- COFACTOR:
Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
Evidence={ECO:0000269|PubMed:8805580};
Note=Contains 1 topaquinone per subunit.
{ECO:0000269|PubMed:8805580};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8805580}.
-!- PTM: Topaquinone (TPQ) is generated by copper-dependent
autoxidation of a specific tyrosyl residue.
{ECO:0000269|PubMed:8805580}.
-!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
{ECO:0000305}.
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EMBL; L39931; AAA62490.1; -; Genomic_DNA.
PIR; A57327; C44239.
PDB; 1KSI; X-ray; 2.20 A; A/B=31-672.
PDB; 1W2Z; X-ray; 2.24 A; A/B/C/D=26-674.
PDBsum; 1KSI; -.
PDBsum; 1W2Z; -.
ProteinModelPortal; Q43077; -.
SMR; Q43077; -.
BindingDB; Q43077; -.
ChEMBL; CHEMBL5534; -.
iPTMnet; Q43077; -.
KEGG; ag:AAA62490; -.
KO; K00276; -.
BRENDA; 1.4.3.21; 4872.
SABIO-RK; Q43077; -.
EvolutionaryTrace; Q43077; -.
GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0052597; F:diamine oxidase activity; IDA:UniProtKB.
GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProtKB-EC.
GO; GO:0048038; F:quinone binding; IEA:InterPro.
GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
GO; GO:0097185; P:cellular response to azide; IDA:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
Gene3D; 2.70.98.20; -; 1.
InterPro; IPR000269; Cu_amine_oxidase.
InterPro; IPR015798; Cu_amine_oxidase_C.
InterPro; IPR036460; Cu_amine_oxidase_C_sf.
InterPro; IPR016182; Cu_amine_oxidase_N-reg.
InterPro; IPR015800; Cu_amine_oxidase_N2.
InterPro; IPR015802; Cu_amine_oxidase_N3.
PANTHER; PTHR10638; PTHR10638; 1.
Pfam; PF01179; Cu_amine_oxid; 1.
Pfam; PF02727; Cu_amine_oxidN2; 1.
Pfam; PF02728; Cu_amine_oxidN3; 1.
SUPFAM; SSF49998; SSF49998; 1.
SUPFAM; SSF54416; SSF54416; 2.
PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
1: Evidence at protein level;
3D-structure; Copper; Disulfide bond; Glycoprotein; Manganese;
Metal-binding; Oxidoreductase; Signal; TPQ.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 674 Primary amine oxidase.
/FTId=PRO_0000035680.
REGION 323 334 Substrate binding.
{ECO:0000250|UniProtKB:P12807}.
REGION 409 414 Substrate binding.
{ECO:0000250|UniProtKB:P46883}.
ACT_SITE 325 325 Proton acceptor.
{ECO:0000250|UniProtKB:P12807}.
ACT_SITE 412 412 Schiff-base intermediate with substrate;
via topaquinone.
{ECO:0000250|UniProtKB:P12807}.
METAL 467 467 Copper; via tele nitrogen.
{ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
METAL 469 469 Copper; via tele nitrogen.
{ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
METAL 476 476 Manganese. {ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
METAL 477 477 Manganese; via carbonyl oxygen.
{ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
METAL 478 478 Manganese. {ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
METAL 617 617 Manganese. {ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
METAL 618 618 Manganese; via carbonyl oxygen.
{ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
METAL 628 628 Copper; via pros nitrogen.
{ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
MOD_RES 412 412 2',4',5'-topaquinone.
{ECO:0000244|PDB:1KSI,
ECO:0000269|PubMed:8805580}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 583 583 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1W2Z}.
DISULFID 162 183 {ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
DISULFID 344 370 {ECO:0000244|PDB:1KSI,
ECO:0000244|PDB:1W2Z,
ECO:0000269|PubMed:8805580}.
HELIX 40 53 {ECO:0000244|PDB:1KSI}.
TURN 56 58 {ECO:0000244|PDB:1KSI}.
STRAND 61 68 {ECO:0000244|PDB:1KSI}.
HELIX 73 81 {ECO:0000244|PDB:1KSI}.
HELIX 83 85 {ECO:0000244|PDB:1KSI}.
STRAND 91 98 {ECO:0000244|PDB:1KSI}.
STRAND 101 108 {ECO:0000244|PDB:1KSI}.
TURN 109 112 {ECO:0000244|PDB:1KSI}.
STRAND 113 119 {ECO:0000244|PDB:1KSI}.
HELIX 130 136 {ECO:0000244|PDB:1KSI}.
HELIX 137 142 {ECO:0000244|PDB:1KSI}.
HELIX 144 152 {ECO:0000244|PDB:1KSI}.
HELIX 157 159 {ECO:0000244|PDB:1KSI}.
STRAND 160 165 {ECO:0000244|PDB:1KSI}.
STRAND 178 185 {ECO:0000244|PDB:1KSI}.
HELIX 192 194 {ECO:0000244|PDB:1KSI}.
STRAND 195 197 {ECO:0000244|PDB:1KSI}.
STRAND 199 205 {ECO:0000244|PDB:1KSI}.
TURN 206 209 {ECO:0000244|PDB:1KSI}.
STRAND 210 216 {ECO:0000244|PDB:1KSI}.
HELIX 232 234 {ECO:0000244|PDB:1W2Z}.
STRAND 246 249 {ECO:0000244|PDB:1KSI}.
STRAND 257 259 {ECO:0000244|PDB:1KSI}.
STRAND 262 265 {ECO:0000244|PDB:1KSI}.
STRAND 268 275 {ECO:0000244|PDB:1KSI}.
TURN 276 278 {ECO:0000244|PDB:1KSI}.
STRAND 279 289 {ECO:0000244|PDB:1KSI}.
TURN 290 293 {ECO:0000244|PDB:1KSI}.
STRAND 294 311 {ECO:0000244|PDB:1KSI}.
TURN 316 320 {ECO:0000244|PDB:1KSI}.
HELIX 325 329 {ECO:0000244|PDB:1KSI}.
TURN 331 334 {ECO:0000244|PDB:1KSI}.
TURN 340 342 {ECO:0000244|PDB:1KSI}.
STRAND 349 356 {ECO:0000244|PDB:1KSI}.
STRAND 362 384 {ECO:0000244|PDB:1KSI}.
STRAND 392 409 {ECO:0000244|PDB:1KSI}.
STRAND 412 420 {ECO:0000244|PDB:1KSI}.
STRAND 426 434 {ECO:0000244|PDB:1KSI}.
STRAND 438 440 {ECO:0000244|PDB:1KSI}.
HELIX 446 448 {ECO:0000244|PDB:1KSI}.
STRAND 454 459 {ECO:0000244|PDB:1KSI}.
STRAND 462 465 {ECO:0000244|PDB:1KSI}.
STRAND 467 477 {ECO:0000244|PDB:1KSI}.
STRAND 484 495 {ECO:0000244|PDB:1KSI}.
STRAND 498 500 {ECO:0000244|PDB:1W2Z}.
STRAND 504 513 {ECO:0000244|PDB:1KSI}.
HELIX 517 520 {ECO:0000244|PDB:1KSI}.
STRAND 529 539 {ECO:0000244|PDB:1KSI}.
STRAND 545 551 {ECO:0000244|PDB:1KSI}.
HELIX 565 569 {ECO:0000244|PDB:1KSI}.
HELIX 571 574 {ECO:0000244|PDB:1KSI}.
STRAND 576 581 {ECO:0000244|PDB:1KSI}.
STRAND 599 602 {ECO:0000244|PDB:1KSI}.
HELIX 603 606 {ECO:0000244|PDB:1KSI}.
HELIX 607 609 {ECO:0000244|PDB:1KSI}.
STRAND 614 616 {ECO:0000244|PDB:1KSI}.
STRAND 618 628 {ECO:0000244|PDB:1KSI}.
HELIX 632 634 {ECO:0000244|PDB:1KSI}.
STRAND 635 637 {ECO:0000244|PDB:1KSI}.
STRAND 641 644 {ECO:0000244|PDB:1KSI}.
STRAND 646 651 {ECO:0000244|PDB:1KSI}.
STRAND 653 655 {ECO:0000244|PDB:1KSI}.
TURN 657 660 {ECO:0000244|PDB:1KSI}.
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


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