ID A0A369JIS2_HYPMA Unreviewed; 733 AA.
AC A0A369JIS2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN Name=cao1 {ECO:0000313|EMBL:RDB19304.1};
GN ORFNames=Hypma_013449 {ECO:0000313|EMBL:RDB19304.1};
OS Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB19304.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB19304.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB19304.1,
RC ECO:0000313|Proteomes:UP000076154};
RA Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA Jeong J., Song E.-S.;
RT "Whole genome sequencing of Hypsizygus marmoreus.";
RL Submitted (APR-2018) 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:RDB19304.1}.
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DR EMBL; LUEZ02000080; RDB19304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369JIS2; -.
DR STRING; 39966.A0A369JIS2; -.
DR InParanoid; A0A369JIS2; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000076154; 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; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF86; COPPER AMINE OXIDASE 1-RELATED; 1.
DR Pfam; PF01179; Cu_amine_oxid; 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.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 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:UP000076154};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 133..232
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 291..702
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 708..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 366
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 451
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 451
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 733 AA; 81323 MW; D8B342EE6A70112A CRC64;
MSTTTVPSTV TEVLQSSTKV PLAFKHPLDP LTPDEIAAAS LAVRKHIAAL PEIKAIKFIT
LYLLPAPKRD VLAFLGIPLS PGSKPEEPRP IVRKAEADFL DLVNGGAYNV ILSLIDGEWT
VDTIEKLPEI QQPQISVEEL VEAEGVIKAD ERVRKLAADV GVTPDQIVCD GWSIGYDERF
PQSRRVQQAL VFARFSKHDN LYAHPMDFVP VIDANTLEVI HIDFPPRYKP GPNGPELTIP
STAFPSLTED GFAFSGRERI PPPLGAFNFL PDLQAQDDKE FKPRVVKPLY VVQPDGVGFS
MDGNVLEWQN WKMHISFTQR EGIALSTITY NDNGEVRPLF YRLSLAEMVV PYGAPEYPHP
RKFAFDSGEY GMGTMANQLS LGCDCLGQIH YLPGAFVAHN GSAIVVKNVI CIHEEDDGVL
WKHTDYRPGG RSRTVRRRRL VVSMVCTLAN YEYIWNYYFY QDGGVELEIR LTGVLQVYVS
ADGEPSPYGV HVAPNVNAQY HQHLFSLRVD PMIDGLNNSI VESDIFPVDA PTGSAANFAG
NAFVTKDTIL KTEGGRQFEW EKERRWKIVN TSKKHYSSGL DVGYIIMMKG GATPMMAKPD
SWCAKRAAFC TNAIWVCKDV EGPKGSRMWP SGKYVPQTRE EPEDSIGKWV EGKQNVDNDD
IVVFLTVGTT HIPKPEDWPV MPVEHLNVML KPNSFFKFNP SLDVPSTSDA HSVSAFPSEP
APTGHCATGG ACH
//
