ID A0A395MT47_9HYPO Unreviewed; 748 AA.
AC A0A395MT47;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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=FIE12Z_4693 {ECO:0000313|EMBL:RFN51052.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN51052.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN51052.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN51052.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:RFN51052.1}.
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DR EMBL; PXXK01000121; RFN51052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MT47; -.
DR STRING; 2594813.A0A395MT47; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000265631; 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 PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 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 Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 252..675
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 410
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 410
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 748 AA; 83023 MW; 57FC8D73763EBF57 CRC64;
MAPSKLHPLA QLSQDEFILA RNCVLKHHES GTSLFFRSIQ LQEPGKEDLV PFLIAEHDGS
LTESTPRPAR CAQVEYDIIA DTRDYTRTIV NVDRGEVVSK DVLEKNAHPN MATYEVETFQ
DACVESQLFK DAMSEFTLPE GFAVCIDPWP YGGTFDDGYP SRYMQGLVFG KNVSNNNPDS
NHYAYPIPII PVMDMETKVI IRVDRLATGS SDDDFEAKER GESPTKLFQN SHAAEYVPEL
LDRPLREGLK PLNVTQPEGA SFTISSDGLV EWQKWRFRLS FTPREGAVLH DICYENRSIL
YRLSYSELTV PYSDPRPPFH RKHAFDLGDG GVGRAANNLQ LGCDCLGAIH YVDSYLASPE
GMPTPAKSVI CLHEQDNGVL WKHTNFRTNR AVVTRMRELV VQFIVTLANY EYIFAYKLDL
AGNITIETRA TGVVSVVGID EGKTSRYGNV VAPGVLAQNH QHIFSVRIDP AVDSYSGEDA
QVIVEESVGR PIDPKTNPRG NLYEVERKKV SKASWTDAEP RLNRLIKLEH ASKRNAMSGR
PVAYKLIPPA TQMLLADAES VAAARAPFAQ HNVWFTGYRD GELWAAGEFT NQSKEEVGGV
SDMVKRGDWF TDEDGVEATN GDSEDHKKGR RSSPVVWVSF GLTHNPRVED WPVMPVETHQ
IHLRPADFFT SNPALDVPST KNESSVLVSC CDKIKATEQV KKPLVQENPV SHLQGGGNGI
EARIAGAHVD DGVKARGKGC IALDDLVG
//
