ID A0A1Y2LPM0_EPING Unreviewed; 738 AA.
AC A0A1Y2LPM0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=B5807_10452 {ECO:0000313|EMBL:OSS45472.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS45472.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS45472.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS45472.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(2017).
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}.
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DR EMBL; KZ107854; OSS45472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2LPM0; -.
DR STRING; 105696.A0A1Y2LPM0; -.
DR InParanoid; A0A1Y2LPM0; -.
DR OMA; VHVGFNY; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000193240; Unassembled WGS sequence.
DR GO; GO:0052595; F:aliphatic amine oxidase activity; IEA:RHEA.
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; 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; 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.
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:UP000193240};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 53..136
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 143..244
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 270..682
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 431
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 431
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 738 AA; 82448 MW; D6EA854E565744F3 CRC64;
MDVHKPAGLF SLISIIDKLS SLESCSSSFT TTMALDRLKQ AASHITGQVA PPHPFDPLSE
LEIEAAVALI RKEHPDVFFN AVTLWEPRKL EMMAWIRAPE VAPRPHRVAD VVCIGRGSKV
FDAHVSLTEN KLLSWELTEG VQPLITMEDL QIVETIVRKD PKVIEQCVIL GIPPQDMHKV
YCDPWTVGYD ERFGTNVRLQ QALMYYRPHV DDSQYSFPLD FCPIYNSDTQ EIIHIDIPPV
RRPLNKAPPN NYHAAAIEKE GGFRTDLKPI NITQPEGVSF KVEGRYIIWA NWRLHVGFNY
REGLILSNIT FNDKGTPRDT FWRLSLAEMV VPYGNPDHPH QRKHAFDLGE YGGGYMTNSL
SLGCDCKGAI HYMDAVFVNR AGQATTIKNA ICIHEEDAGI LFKHTDFRDD SVTVTRARKL
IISHIFTAAN YEYCVYWIFH LDGTIQLEIK LTGILNTYAM LPGEDLKGWG TEVYPGVNAH
NHQHLFCLRI DPNIDGPNNT VFMVDAARGD GEVGSAENKY GNAFYAKKTK LSTPEMAATD
YNGATSRTWD MCNENKINPY SKKPSSYKLV SREVPELLPK PGGLVWKRAG FARHAVHVTR
YDDAQLHPAG RHVPQTSGDP SQGIPAWIAA NPTANLENTD VVLWHTFGLT HFPSPEDFPV
MPAEPISLLL RPRNFFTRNP CLDIPPSYCS VPSDVKQGSA LVDRISKLAF GDRETAAAQD
KGLGEPACCS SEKFGAGV
//
