ID A0A103YC01_CYNCS Unreviewed; 776 AA.
AC A0A103YC01;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=Ccrd_015364 {ECO:0000313|EMBL:KVI06294.1};
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:KVI06294.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVI06294.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVI06294.1};
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|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:KVI06294.1}.
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DR EMBL; LEKV01001840; KVI06294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103YC01; -.
DR STRING; 59895.A0A103YC01; -.
DR EnsemblPlants; KVI06294; KVI06294; Ccrd_015364.
DR Gramene; KVI06294; KVI06294; Ccrd_015364.
DR OMA; EMCNESK; -.
DR OrthoDB; 34972at2759; -.
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; 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:SF96; 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:UP000243975};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 77..166
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 202..305
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 331..739
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 409
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 493
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 493
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 776 AA; 86254 MW; 156AF8F06B8B2E05 CRC64;
MASASQKASH SCVDSLPIRR QIVPASASAA ADVVVVEDWN NDDRPLPIKN SVITPTDPSA
NASTKGIQVL TRDQTSHPLD PLSAAEIKVA VATVRAAGAT PEVRDGMRFV EVVLSEPDKN
VVALADAYFF PPFQPSLLPR SKGGAVIPTR LPPRRARLVV YNKKTNETSV WTVELSEVHA
TTRGGHHRGK VISSRVVLDV QPPMDAVEYA ECEAVVKDYP PFREAMKKRG IEDMDLVMVD
AWCVGYHSDA DAPSRRLAKP LIFCRTESDS PMENGYARPV EGIYVLVDMQ NMVVLEFEDR
KLVPLPPADP LRNYTPGHTR GGVDRSDVKP LQILQPHGPS FRVNGHYVEW QKWNFRIGFT
PREGLVIHSV AYVDGSRGRR PIAHRLSFVE MVVPYGDPND PHYRKNAFDA GEDGLGKNAH
SLKKGCDCLG YIKYFDAHFT NFIGGVETIE NCVCMHEEDH GILWKHQDWR TGLAEVRRSR
RLTVSFICTV ANYEYGFYWH FYQDGKIEAE VKLTGILSLG ALQPGEVRKY GTTIAPGLYA
PVHQHFFVAR MDMAVDCKAG EAYNQVVEVD VKVEEPGKDN VHNNAFYTQE TLLKSESQAM
RDCNPLSARH WIVKNTRTVN RTGQLTGYKL VPGSNCLPLA GSEAKFLRRA AFLKHNLWVT
PYASGEDFPG GEFPNQNPRV GEGLASWVQQ NRSLEETDIV LWYVFGITHV PRLEDWPVMP
VERIGFMLQP HGFFNCSPAV DVPPGACESD VKDSSSHVKD AIAPKAVSNG LIAAKL
//
