ID A0A0P7ATH7_9HYPO Unreviewed; 793 AA.
AC A0A0P7ATH7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=AK830_g10382 {ECO:0000313|EMBL:KPM36184.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM36184.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM36184.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM36184.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) 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:KPM36184.1}.
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DR EMBL; LKCW01000215; KPM36184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7ATH7; -.
DR STRING; 78410.A0A0P7ATH7; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
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; IPR015328; DUF1965.
DR PANTHER; PTHR10638:SF20; 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; PF09248; DUF1965; 1.
DR PRINTS; PR00766; CUDAOXIDASE.
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:UP000050424};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..793
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006135057"
FT DOMAIN 76..152
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 246..313
FT /note="DUF1965"
FT /evidence="ECO:0000259|Pfam:PF09248"
FT DOMAIN 325..725
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 398
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 479
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 479
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 793 AA; 88126 MW; 07DE0FF6B8E66566 CRC64;
MRLIVCLELC LLPLLGQASA RPGISGPAAR PHSLNRLSTR NSEAAASGCS AGKDVLITAP
KKNIFQSLTD TEYADVTAFL HEQNELNLTA VVNSTSWDNV IVTMDLLQPN KTGALAYLDE
DAKAPTRYAR ATLQFNSKVQ PYLQEYMVGP LPIKKGSARY EELNYIFTSG RGRTNVYNAD
GEAIAAFNLE VGKEIKDITK KLLNGTATGA DDDNLLIAGS DPLIHSGNRI YQWNEFYSAH
TGEFFSETIL PTSLQFKIDI TGRDPSKWRV VGWYYDGDYW PTTAAFRKAS KTLTRKPGPN
VDGSWTATDQ LGEKLPRDHL YPPISIQPDG PRFGVDKKEN YVEWMDFSFY ISNHREVGMQ
LHDIRYKGER LIYEFGLQEA LAHYASQDPL HASSAYLDTS YGMGTSQWNL VDGFDCPSHA
TYLNTTFYIS ETTHVHPNSL CLFEYDAGFP IQRHLTGTHV SATKNIIFTV RAVSTVGNYD
YLFEYSFHYD GSIAVTVRAS GYIQGAFWSG DGDYGFHIHD NLSGSMHDHV LNFKLDLDIK
GRKNSLLKTE FVPATEVYPW SDGQSINTMK VNRSYITNED DSKITWSKNG AAAYAVVNKD
QLNKFGEAPG YRISPNSGST AYLTVQSSSS LGQSANWANH NLYALQHHDT EPKSAYAFNS
HDPHHPAVNF DDFFNGESLD QEDIVLYFNL GMHHIPNTAD LPNTVTTTAM SSIAISPQNY
FAGDVSRRTI HGVRLSYNET SAITDKKTFG TKQPTCAYDM KKAAPDLNSF VGEIEIAKFP
WNPSGSLQTN PGG
//
