ID A0A118JSD4_CYNCS Unreviewed; 732 AA.
AC A0A118JSD4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=Ccrd_024672 {ECO:0000313|EMBL:KVH88959.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH88959.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH88959.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH88959.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
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|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:KVH88959.1}.
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DR EMBL; LEKV01005325; KVH88959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A118JSD4; -.
DR STRING; 59895.A0A118JSD4; -.
DR EnsemblPlants; KVH88959; KVH88959; Ccrd_024672.
DR Gramene; KVH88959; KVH88959; Ccrd_024672.
DR Proteomes; UP000243975; 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 Gene3D; 3.10.450.40; -; 2.
DR Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 2.
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; 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; 2.
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:UP000243975};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|RuleBase:RU000672}.
FT DOMAIN 206..317
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 343..495
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT DOMAIN 496..691
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
SQ SEQUENCE 732 AA; 80904 MW; 66C602416C90DE8B CRC64;
MASTSEKATS LLLREVTSSS AADVVQDWTT DPSVGDQIRH RGTATSVGDL IRPVVAQSSA
ATAAAKGGTG PTSMVRAQTR HPLDPLAAAE ISIAVATVRA AGATPEVRDS MRFIEVVLVE
PAKSVVALAD AYFFPPFQPS LLPRTKGGPI IPTKLPPRQA RLIVYNKKSN ETSIWIVELS
EVHALTRGGH HRGKVISSKV VPDVQPPMDA VEYAECEAIV KDFPPFREAM KRRGIEDMDL
VMMLMLRMPN LYFRCVGYHS EADAPKRRLA KPLIFCRTES DCPMENGYAR PVEGIDVLVD
MQNMVVIEFK DRKLVPLPPA DPLRNYTAGE TRGGVDRSDV KPLNIIQPDG PSFRVDGHFV
QWQKWNFRIG FTPREGLVIY SVAYVDGSRG RRPVAHRLSF VEMVVPYGDP NDPHYRKNAF
DAGEDGLGKN AHSLKKGCDC LGYVKYFDAH LTNFTGGVET IEDCVCLHEE DHGILWKHQD
WRTGLAEVRR SRRLVDGKIE AEVKLTGILS LGALQPGEAR KYGTMIAPGL YAPVHQHFFV
ARMDMSVDCK PGESHNQVVE LDVKVEGPGD ANVHNNAFYA EEKLLKSELE AMRDCNPSSA
RHWVIRNTRT VNRTGQLTGY KLVPGSNCLP LGGAEAKFLR RAAFLMHNLW VTPYKSDEMF
PGGEFPNQNP RVGEGLATWV KQNRSLEETD LPHGFFNCSP AVDVPPSSLA DLELKENGMV
EKACHNGLVS KM
//
