AMO_LENCU
ID AMO_LENCU Reviewed; 667 AA.
AC P49252; Q9LD03;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Primary amine oxidase;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P46883};
DE AltName: Full=Amine oxidase [copper-containing];
DE Flags: Precursor; Fragment;
OS Lens culinaris (Lentil) (Cicer lens).
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; Lens.
OX NCBI_TaxID=3864;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-66 AND 543-562.
RC TISSUE=Seedling;
RX PubMed=1577161; DOI=10.1016/0014-5793(92)80251-b;
RA Rossi A., Petruzzelli R., Finazzi Agro A.;
RT "cDNA-derived amino-acid sequence of lentil seedlings' amine oxidase.";
RL FEBS Lett. 301:253-257(1992).
RN [2]
RP SEQUENCE REVISION TO 444-667.
RX PubMed=7622512; DOI=10.1074/jbc.270.28.16939;
RA Tipping A.J., McPherson M.J.;
RT "Cloning and molecular analysis of the pea seedling copper amine oxidase.";
RL J. Biol. Chem. 270:16939-16946(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA McPherson M.J.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 24-35; 258-276 AND 360-377.
RX PubMed=1397633; DOI=10.1042/bst0200369;
RA Agro A.F., Rossi A.;
RT "Copper-containing plant oxidases.";
RL Biochem. Soc. Trans. 20:369-373(1992).
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: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=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=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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46883}.
CC -!- PTM: Glycosylated; contains two carbohydrate chains per monomer.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA45526.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X64201; CAA45526.1; ALT_FRAME; mRNA.
DR EMBL; S78994; AAB34918.3; -; mRNA.
DR PIR; S21139; S21139.
DR AlphaFoldDB; P49252; -.
DR SMR; P49252; -.
DR KEGG; ag:AAB34918; -.
DR BRENDA; 1.4.3.21; 2969.
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: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 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 Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Metal-binding; Oxidoreductase; Signal; TPQ.
FT SIGNAL <1..18
FT /evidence="ECO:0000269|PubMed:1577161"
FT CHAIN 19..667
FT /note="Primary amine oxidase"
FT /id="PRO_0000035679"
FT REGION 216..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 405
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 316..327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 402..407
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 460
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 462
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 469
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 470
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 471
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 610
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 611
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 621
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MOD_RES 405
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 155..176
FT /evidence="ECO:0000250"
FT DISULFID 337..363
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CONFLICT 492..496
FT /note="GGSKR -> EVQE (in Ref. 1; CAA45526)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="Y -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="V -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="R -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ 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
