ID A0A1Q3CFA0_CEPFO Unreviewed; 800 AA.
AC A0A1Q3CFA0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=CFOL_v3_22379 {ECO:0000313|EMBL:GAV78914.1};
OS Cephalotus follicularis (Albany pitcher plant).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV78914.1, ECO:0000313|Proteomes:UP000187406};
RN [1] {ECO:0000313|Proteomes:UP000187406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA Fukushima K., Hasebe M., Fang X.;
RT "Cephalotus genome sequencing.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000672};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000256|RuleBase:RU000672};
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC ECO:0000256|RuleBase:RU000672}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAV78914.1}.
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DR EMBL; BDDD01001881; GAV78914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3CFA0; -.
DR STRING; 3775.A0A1Q3CFA0; -.
DR InParanoid; A0A1Q3CFA0; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000187406; Unassembled WGS sequence.
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: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:UniProtKB-UniRule.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR Gene3D; 3.10.450.40; -; 2.
DR Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 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:SF18; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 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; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000672};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000672};
KW Reference proteome {ECO:0000313|Proteomes:UP000187406};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 107..194
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 232..335
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 361..770
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 523
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 523
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 800 AA; 88695 MW; BB729AC0AF2AD7FC CRC64;
MATTQEKATP PCCNIHASNA SSSPATTSTT TTSRPLLRNA SAAVATDAKL LPNWSITGSD
ASVGPARERA SLSTLIRPVE SLSDSPTAAK PTSTIGMPIM LKAQSSHPLD PLSAAEISVA
VATVRAAGAT PEVRDSMRFV EVVLLEPGKQ VVALADAYFF PPFQPSLLPR TKGGPVIPSK
LPPRQARLVV YNKRSNDTSI WIVELSEVHA ATRGGHHRGK VISSKVVPNV QPPMDAEEYA
ECEAVVKDFP PFREAMKKRG IEDMDLVMVD PWCAGYHSEA DAPSRRLAKP LVFCRTESDC
PLENGYARPV EGIHVLVDMQ NMVVVEFEDR KLVPLPPADP LRNYGSAESR GGVDRSDVKP
LHIIQPEGPS FRVNGHFIEW QKWNFRIGFT PREGLVIYSV AYVDGSRGRR PVAHRLSFVE
MVVPYGDPND PHYRKNAFDA GEDGLGKNAH SLKKGCDCLG YIKYFDAHFQ NFTGGVETIE
KCVCLHEEDH GILWKHQDWR TGLAEVRRSR RLTVSFICTV ANYEYGFFWH FYQARGKIEA
EVKLTGILSL GALLPGEIRK YGTTIAPGLY APVHQHFFVA RMDMAVDCKP GETHNQVVEL
NVKVEEPGKD NVHNNAFYAE EELLTSELQA MRDCNPLTAR HWIIRNTRTV NRTGQLTGYK
LVPGSNCLPL AGSEAKFLRR AAFLKHNIWV TPYARDEMYP GGEFPNQNPR VGEGLATWVK
QNRSLEETDI VLWYVFGITH IPRLEDWPVM PVDRIGFMLM PHGFFNCSPA VDVPPSSIDL
ELKDNGIAAK PIQNGLLAKL
//
