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

 AMO_LENCU               Reviewed;         667 AA.
P49252; Q9LD03;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 3.
20-DEC-2017, entry version 91.
RecName: Full=Primary amine oxidase;
EC=1.4.3.21 {ECO:0000250|UniProtKB:P46883};
AltName: Full=Amine oxidase [copper-containing];
Flags: Precursor; Fragment;
Lens culinaris (Lentil) (Cicer lens).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Lens.
NCBI_TaxID=3864;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-66 AND 543-562.
TISSUE=Seedling;
PubMed=1577161; DOI=10.1016/0014-5793(92)80251-B;
Rossi A., Petruzzelli R., Finazzi Agro A.;
"cDNA-derived amino-acid sequence of lentil seedlings' amine
oxidase.";
FEBS Lett. 301:253-257(1992).
[2]
SEQUENCE REVISION TO 444-667.
PubMed=7622512; DOI=10.1074/jbc.270.28.16939;
Tipping A.J., McPherson M.J.;
"Cloning and molecular analysis of the pea seedling copper amine
oxidase.";
J. Biol. Chem. 270:16939-16946(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
McPherson M.J.;
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 24-35; 258-276 AND 360-377.
PubMed=1397633; DOI=10.1042/bst0200369;
Agro A.F., Rossi A.;
"Copper-containing plant oxidases.";
Biochem. Soc. Trans. 20:369-373(1992).
-!- CATALYTIC ACTIVITY: RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) +
H(2)O(2). {ECO:0000250|UniProtKB:P46883}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000250|UniProtKB:P46883};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P12807};
Note=Binds 1 copper ion per subunit (By similarity). Can also use
zinc ion as cofactor (By similarity).
{ECO:0000250|UniProtKB:P12807, ECO:0000250|UniProtKB:P46883};
-!- COFACTOR:
Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
Evidence={ECO:0000250|UniProtKB:P46883};
Note=Contains 1 topaquinone per subunit.
{ECO:0000250|UniProtKB:P46883};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q43077};
Note=Binds 1 Mn(2+) ion per subunit.
{ECO:0000250|UniProtKB:Q43077};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46883}.
-!- PTM: Glycosylated; contains two carbohydrate chains per monomer.
-!- PTM: Topaquinone (TPQ) is generated by copper-dependent
autoxidation of a specific tyrosyl residue.
{ECO:0000250|UniProtKB:P46883}.
-!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA45526.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X64201; CAA45526.1; ALT_FRAME; mRNA.
EMBL; S78994; AAB34918.3; -; mRNA.
PIR; S21139; S21139.
ProteinModelPortal; P49252; -.
SMR; P49252; -.
PRIDE; P49252; -.
KEGG; ag:AAB34918; -.
KO; K00276; -.
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: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.
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;
Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
Metal-binding; Oxidoreductase; Signal; TPQ.
SIGNAL <1 18 {ECO:0000269|PubMed:1577161}.
CHAIN 19 667 Primary amine oxidase.
/FTId=PRO_0000035679.
REGION 316 327 Substrate binding.
{ECO:0000250|UniProtKB:P12807}.
REGION 402 407 Substrate binding.
{ECO:0000250|UniProtKB:P46883}.
ACT_SITE 318 318 Proton acceptor.
{ECO:0000250|UniProtKB:P12807}.
ACT_SITE 405 405 Schiff-base intermediate with substrate;
via topaquinone.
{ECO:0000250|UniProtKB:P12807}.
METAL 460 460 Copper; via tele nitrogen.
{ECO:0000250|UniProtKB:P12807}.
METAL 462 462 Copper; via tele nitrogen.
{ECO:0000250|UniProtKB:P12807}.
METAL 469 469 Manganese.
{ECO:0000250|UniProtKB:Q43077}.
METAL 470 470 Manganese; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q43077}.
METAL 471 471 Manganese.
{ECO:0000250|UniProtKB:Q43077}.
METAL 610 610 Manganese.
{ECO:0000250|UniProtKB:Q43077}.
METAL 611 611 Manganese; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q43077}.
METAL 621 621 Copper; via pros nitrogen.
{ECO:0000250|UniProtKB:P12807}.
MOD_RES 405 405 2',4',5'-topaquinone.
{ECO:0000250|UniProtKB:P12807}.
CARBOHYD 149 149 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 576 576 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 155 176 {ECO:0000250}.
DISULFID 337 363 {ECO:0000250|UniProtKB:P12807}.
CONFLICT 492 496 GGSKR -> EVQE (in Ref. 1; CAA45526).
{ECO:0000305}.
CONFLICT 575 575 Y -> N (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 651 651 V -> A (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 658 658 R -> I (in Ref. 1; AA sequence).
{ECO:0000305}.
NON_TER 1 1
SEQUENCE 667 AA; 75558 MW; ED9A415C7E4F7AEC CRC64;
KFALFSVLTL LSFHAVFSFT PLHTQHPLDP ITKEEFLAVQ TIVQNKYPIS NNKLAFHYIG
VDDPEKDLVL KYETSPTLIS IPRKIFVVAI INSQTHEILI DLTIKSIVSD NIHNGYGFPV
LSAAEQFLAI DLPLKYPPFI ASVNKRGLNI SEIVCSSFTM GWFGEEKNSR TVRVDCFMKE
STVNIYVRPI TGITIVADLD LMKIVEYHDR DTEAVPTAEN TEYQVSKQSP PFGPKQHSLT
SHQPQGPGFQ INGTSVSWAN WKFHIGFDVR AGIVISLASI YDLEKHKSRR VLYKGYISEL
FVPYQDPTEE FYFKTFFDSG EFGFGLSTVS LIPNRDCPPH AQFIDTYIHS ADGTPIFLEN
AICVFEQYGN IMWRHTETGI PNESIEESRT EVDLAIRTVV TVGNYDNVLD WEFKTSGWMK
PSIALSGILE IKGTNIKHKD EIKEEIHGKL VSANSIGIYH DHFYIYYLDF DIDGTQNSFE
KTSLKTVRIV DGGSKRKSYW TTETQTAKTE SDAKITIGLA PAELVVVNPN IKTAVGNEVG
YRLIPAIPAH PLLTEDDYPQ IRGAFTNYNV WVTPYNRTEK WAGGLYVDHS RGDDTLAVWT
KKNREIVNKD IVMWHVVGIH HVPAQEDFPI MPLLSTSFEL RPTNFFERNP VLKTLPPRDF
TWPGCSN


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