ID A0A1V8T0K3_9PEZI Unreviewed; 694 AA.
AC A0A1V8T0K3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=B0A48_09671 {ECO:0000313|EMBL:OQO04748.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO04748.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:OQO04748.1}.
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DR EMBL; NAJO01000021; OQO04748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8T0K3; -.
DR STRING; 1507870.A0A1V8T0K3; -.
DR InParanoid; A0A1V8T0K3; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000192596; 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:UP000192596};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 22..104
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 111..212
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 238..650
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 315
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 399
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 399
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 694 AA; 77002 MW; D551519136FF3252 CRC64;
MVLERLQQVA SHLAGHTNPS NPFDPLSTEE IAAAVAIVRQ SHPDVFFNTV TLWEPRKEEM
MRYVASPETV PRPHRIADVV AIGRGSKVFD GTVDLIEGKI VTWDLTEGVQ PLITMEDLQI
VETVVRKDAK VIEQCGIVGI PPQDMHKVYC DPWTIGYDER FGSGVRLQQA LMYYRPHIDD
SQYTYPLDFC PIYNSDTQEI VHIDIPKVRR PLNTAPPTNY HAEAIKAAGG FRTDLKPINI
SQPEGVSFTV DGRTVKWQNW SCHVGFNYRE GIVLSNVTFN DKGTVRPIFW RISLAEMVVP
YGNPERPHHR KHAFDLGEYG GGYMTNSLSL GCDCKGAIHY LDAAFVSRNG DPQTIKNAIC
IHEEDAGILF KHTDFRDNST TVTRARKLLI SQIFTAANYE YCVYWILHQD GTIQLEIKLT
GILNTYALNP GESAAPWGTE VYPGVNAHNH QHLFCLRVDP NIDGPNNTIS IVDAVAAEAP
VGSEENFYGN AFYAKKTKVE TMKEGMSDYD GASSRTWEMA NEGKINAYSK KPVGYKLVSR
EVPKLLPKEG SLVWKRAGFA RHAVHVTKYS DEQIHPAGRH VPQTSGEPSQ GLPAWIAADP
EGSLVNTDVV LWHTFGLTHF PAPEDYPVMP AEPMTVLLRP RGFFTENPAM DVPPSYSSTP
SQVAAKKQGL TGVVDSLSRL AFGGTAEKGG SKDA
//
