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Database: UniProt
Entry: A0A3N4JP31_9PEZI
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Original site: A0A3N4JP31_9PEZI 
ID   A0A3N4JP31_9PEZI        Unreviewed;       732 AA.
AC   A0A3N4JP31;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=L873DRAFT_1789218 {ECO:0000313|EMBL:RPA99992.1};
OS   Choiromyces venosus 120613-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Choiromyces.
OX   NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA99992.1, ECO:0000313|Proteomes:UP000276215};
RN   [1] {ECO:0000313|EMBL:RPA99992.1, ECO:0000313|Proteomes:UP000276215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=120613-1 {ECO:0000313|EMBL:RPA99992.1,
RC   ECO:0000313|Proteomes:UP000276215};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(2018).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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}.
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DR   EMBL; ML120383; RPA99992.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4JP31; -.
DR   STRING; 1336337.A0A3N4JP31; -.
DR   Proteomes; UP000276215; 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   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
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:UP000276215};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          27..93
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          271..671
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        344
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        428
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         428
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   732 AA;  82372 MW;  15BAD8F542271DE7 CRC64;
     MRPEPRGSVT QTVSEKLNIY LSTPPPHPLD QLSLDEINKT RDVILRAHSS SSIVFRTITL
     EEPAKVLLLP FLQAEHRGEV TNRTRRPPRL ARVLFDAIEE DRSLELCDSV VDVRLGEEVS
     FDLIEKKYHS PLNADEIAIF PEVAMASPLF QEALAELNLP TNVVIVIDPW MYGGWDKPKE
     TSPRYMQGLV YARDPKTNNP DSNHYAFPIP LIPVMDIYKR EIVRVDKLAT GGRNDGLKYG
     TGPKNALDHC RAVEYIPELV EGGLRQDVKP LNVIQPYGPS FTTTGSLVEW QKWRFRIGFN
     PREGATIHDV WYDNRSVFYR MSFSEMSVPY GDPRAPFHRK QAFDFGDGGA GRAANNLELG
     CDCLGLIKYF DGIMNDTSGK GIVSKNVVCM HEIDDGILWK HTNYRTNRAV VTRNRKLIVQ
     FIITLANYEY IFAYHFDQAG GITIETRATG VVSTVPIDPG TTSPWGNVVS PGALAQNHQH
     IFCVRIDPAI EGSKNTVIQE ESHPVPFTPE LNPWGNAYEV RQTMFKKTCW ADAAPHNARL
     FKIVNQNVRN PISGKPVGYK LVPSPSQLTL AHPDSIMAKR MAYASHHLWV TRYHDGEFWA
     AGRFTNQSSV ESGGVKDMTE RNENIENEDL VIWHSFGLTH NPRVEDFPVM PIETHQIHLK
     PADFFTKNPA IDVPSTKNQT SILYKVGGLV SGFVAEVPQN NKESERTRQA KIVTVEDNST
     EQLAQGIKSC CM
//
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