ID A0A365NIL5_GIBIN Unreviewed; 683 AA.
AC A0A365NIL5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=FPRO05_08101 {ECO:0000313|EMBL:RBA20654.1};
OS Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=948311 {ECO:0000313|EMBL:RBA20654.1, ECO:0000313|Proteomes:UP000251714};
RN [1] {ECO:0000313|EMBL:RBA20654.1, ECO:0000313|Proteomes:UP000251714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 2341 {ECO:0000313|EMBL:RBA20654.1,
RC ECO:0000313|Proteomes:UP000251714};
RA Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA Sreenivasaprasada S.;
RT "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT strain ITEM 2341 from Date Palm.";
RL Submitted (DEC-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:RBA20654.1}.
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; PKMI01000008; RBA20654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365NIL5; -.
DR Proteomes; UP000251714; 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; IPR015800; Cu_amine_oxidase_N2.
DR PANTHER; PTHR10638:SF33; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 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.
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 TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 7..100
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 244..652
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 206..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 401
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 401
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 683 AA; 77215 MW; 66960892694C35E1 CRC64;
MTTASPHPFD PLSPEEISRA SRIARPHFGN HDPNFRVITL LEPVKKEMIT YLEKEHLNQP
IDHVPTRHAR VEASIKAETE GNHLFELIVD LDADKVVKKQ HVEGKHSYID TDYMKAVEAA
CLANEEVQAM IKTLDLPEGA TVVVEPWAYA TDGMNDMTHR VSMCWFYARL LENPNANYYA
YPLDVCAEVS ESLGVMKVYR LPTTPDERAN NEKRPFDRRR VHSPTNSEYH PDLRPNPRTT
TKPLHITQPE GPSFHIEGNR LTWEKWDLRV GFNYREGLTL HDVRYDGRSL FYRLSLAEMF
VPYGDPRAPY PRKAAFDLGN DGAGINANNL QLGCDCLGTI KYFDAYHNTS SGEPLKLPNV
VCCHEQDDGI LWKHTNFRTN VPVVTRSRIL VLQTIITVTN YEYIFAWHFS QDASIFYEVR
ATGILSTAPT SMDHKGTYPY GNIVAPGVLA PYHQHLFSLR IDPAIDGHAN SLVVEESKPL
PIEDPAIHNP FGVGYVTESQ TVEEEGGFDL DFTKARTFKF VNENKINPIT GTPVGFKLMP
FYSQMLLAHP ESFHAKRSEF AEHAVWVTRY EDNDHFPAGK YTMQSAGGDG LASVIARRRN
TGVAHSVRNE DIVIWHTFGS THNPRIEDWP VMPSEKMMVG LKPVNFFSGN PGLDVAPSTQ
EKNKSVLYTG EDKKDSTCCI SKL
//
