ID A0A2K0VV02_GIBNY Unreviewed; 791 AA.
AC A0A2K0VV02;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=FNYG_12800 {ECO:0000313|EMBL:PNP73841.1};
OS Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP73841.1, ECO:0000313|Proteomes:UP000236664};
RN [1] {ECO:0000313|EMBL:PNP73841.1, ECO:0000313|Proteomes:UP000236664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS10214 {ECO:0000313|EMBL:PNP73841.1,
RC ECO:0000313|Proteomes:UP000236664};
RA Gardiner D.M., Obanor F., Kazan K.;
RT "Genome of Fusarium nygamai isolate CS10214.";
RL Submitted (JUN-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:PNP73841.1}.
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DR EMBL; MTQA01000241; PNP73841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0VV02; -.
DR STRING; 42673.A0A2K0VV02; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000236664; 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 InterPro; IPR015328; DUF1965.
DR PANTHER; PTHR10638:SF20; 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 Pfam; PF09248; DUF1965; 1.
DR PRINTS; PR00766; CUDAOXIDASE.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
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:UP000236664};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..791
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014320039"
FT DOMAIN 74..150
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 244..311
FT /note="DUF1965"
FT /evidence="ECO:0000259|Pfam:PF09248"
FT DOMAIN 322..724
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 396
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 477
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 477
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 791 AA; 88572 MW; A8E6E7D375E40449 CRC64;
MRHPISLILC FVTFLGGIIA YPGLPGPATR PHSLKRLSEY KPSTAGCNFG KDVTIKAPVE
NIFQSLTDEE YAHVTAYLHE QKDLNLTAVV NSTSWDNVIV TLDLLQPNKT DALAYLDGHG
PAPVRYARAT LQFNSKVQPY IQEYMVGPLP FQHDVTQHQE LNYLFTSDRG RINVYNADTE
AIAAFNLKIG AEIKDITKEL LNGTATGDKT DNLLIAGSDP LIHRHGRVYQ WNEFYSAHTG
EFYSETVLPT SLQFKVDLTG RDPSKWKVVG WYYDGHFWPT TAAFCKAIKT LKRKPGPVVD
GSWTSTDQQG DSFPRDHLFP PVSVQPDGPR FGVDREQNYV EWMDFTFFLS NHKETGLQLH
DVRFKGERII YEFGLQEALA HYASQDPLHA SSAYLDSSYG IGTSQWNLVD GFDCPSHATY
LNTTFYISET THVHPNSLCL FEYDTGYPIQ RHLTMDHVSA TKNIVFTVRS VSTVGNYDYL
FEYTFHYDGS IAVTVRASGY IQGAFWSGDG DYGYHIHDNL SGSMHDHVIN FKLDLDVNGR
KNSLMKSEFV PHTQVYPWSD GQPINTMKVN HSYIASEDDG KINWAPNGAT SYSVVNRDKL
NDFGEAPGYS ITPNSGSTAH LTVQSSSALG QAANWANHNL YALQHHDTEP KSAYAFNSHD
LHHPAVDFNK FFNGESLDQE DIVLYFNLGM HHLPNTADLP NTVTTKAVSS MMISPQNYFS
GDVSRRTVHQ VRMSFDKNSN VTEVKRFGVK QPTCAIDMNS VAPDLSTFVG EIEIPKFPWN
PSGSLQTNPG G
//
