ID A0A2R6S670_9APHY Unreviewed; 374 AA.
AC A0A2R6S670;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 22-FEB-2023, entry version 10.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=PHLCEN_2v388 {ECO:0000313|EMBL:PSS37787.1};
OS Hermanssonia centrifuga.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Meruliaceae; Hermanssonia.
OX NCBI_TaxID=98765 {ECO:0000313|EMBL:PSS37787.1, ECO:0000313|Proteomes:UP000186601};
RN [1] {ECO:0000313|EMBL:PSS37787.1, ECO:0000313|Proteomes:UP000186601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC195 {ECO:0000313|EMBL:PSS37787.1,
RC ECO:0000313|Proteomes:UP000186601};
RA Granchi Z., Peng M., de Vries R.P., Hilden K., Makela M.R., Grigoriev I.,
RA Riley R.;
RT "Genome sequence of the basidiomycete white-rot fungus Phlebia
RT centrifuga.";
RL Submitted (FEB-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|RuleBase:RU000672}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {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:PSS37787.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLYV02000031; PSS37787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6S670; -.
DR STRING; 98765.A0A2R6S670; -.
DR Proteomes; UP000186601; 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; 2.70.98.20; Copper amine oxidase, catalytic domain; 2.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR PANTHER; PTHR10638:SF20; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 2.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|RuleBase:RU000672};
KW Metal-binding {ECO:0000256|RuleBase:RU000672};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000672};
KW Reference proteome {ECO:0000313|Proteomes:UP000186601};
KW TPQ {ECO:0000256|RuleBase:RU000672}.
FT DOMAIN 27..78
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT DOMAIN 84..295
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 355..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 41716 MW; 3473D80FC7F65484 CRC64;
MNDTAWATRH RPNTSAARDL DHLPGPRQVS FAGLRFRVDA DLQYVSWMGW GMYLGFDRDM
GLSLWDLRFL GGRIIYEVCS VRSTISALTV GSLHDHVINF KVDLDVAGTD NSLLYTHTVQ
EEVIHPWLDD DWGQTVIQQR IVHEYIQDEN KALLKFPENH RGGYAIVNQA EPNRWGVPRG
YAIRPGYSPI YNTVVGSKRL LHNANWARYN LAISRRKDTE PSSSSTWNLN LPGAPTVDFH
KFFNGENITQ QDLVAWINVG MHHLPQAEDV PNTRANIATS SFFLTPLNYF DSDVSIDSTN
AILINASTEG APSNIDEYGV AAVQCMPEMV PPYHNIKLKA FALDYGEPAP VPVPAATGGG
LGRLGELRDV QDDG
//
