ID A0A136ILC5_9PEZI Unreviewed; 481 AA.
AC A0A136ILC5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, 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 ORFNames=Micbo1qcDRAFT_169429 {ECO:0000313|EMBL:KXJ85429.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ85429.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) 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|RuleBase:RU000672}.
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DR EMBL; KQ964282; KXJ85429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136ILC5; -.
DR STRING; 196109.A0A136ILC5; -.
DR InParanoid; A0A136ILC5; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000070501; 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; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
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 SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 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:UP000070501};
KW TPQ {ECO:0000256|PIRSR:PIRSR600269-50, ECO:0000256|RuleBase:RU000672}.
FT DOMAIN 17..432
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 457..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 179
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 179
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 481 AA; 53558 MW; 9B024CF9AB344A21 CRC64;
MPEFVRDGYM NRLKPIDITQ PEGVSFRMRG NELSWANFRM HVGFNYREGI VLSDIRVDDD
EQGRERTLFN RLSVVEMVVP YGDPNPPHHR KHAFDVGEYG TGLMTNSLKL GCDCKGAIHY
LDAVVATVSG EAALIQNAIC IHEEDNGLLY KHTDYRDGSV ISARDRKLIL SQIITAANYE
YAFYHIFSLD GTYKLEIKLT GQLNTYCMHP SETAAPYGTE VAHRVNAHNH QHIFSLRVDP
AVDGPNNTVV QSDAVASEHP TGSPENPYGN GFYAKKTPFR TAKESVADYC HETSRTWDIT
NPSSINSASH KPVAYKILNN NCPRLLAHAD SKLAKRAHFA RHALFVTPYR DYELFPAGDY
VCQSTGGLDH PHNSTVADWV ARDESIDNTD IVCYVQFGLT HFPRTEDFPI MPAEPVGVML
RASNFFTRNP ALWVPPSTVS VDRSSRNAFA DSKQQQEASA AAVQGPTKSC CAGESRIGSK
L
//