ID M7TMW6_EUTLA Unreviewed; 815 AA.
AC M7TMW6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=UCREL1_4952 {ECO:0000313|EMBL:EMR68050.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR68050.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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}.
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DR EMBL; KB706313; EMR68050.1; -; Genomic_DNA.
DR RefSeq; XP_007792865.1; XM_007794674.1.
DR AlphaFoldDB; M7TMW6; -.
DR STRING; 1287681.M7TMW6; -.
DR KEGG; ela:UCREL1_4952; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_015739_0_0_1; -.
DR OMA; PYNSQDV; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000012174; 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:UP000012174};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..815
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004085830"
FT DOMAIN 97..173
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 268..336
FT /note="DUF1965"
FT /evidence="ECO:0000259|Pfam:PF09248"
FT DOMAIN 347..748
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 502
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 502
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 815 AA; 92325 MW; 6A25B2FFE3C3287A CRC64;
MRVSAVSRPW ATATTALAFL SFAEDVYCRP NPEPKVPARV KWANNRGKKI ARTVLKQSLE
GRQWNTTESC GESTAAKITA PHDNIWGGLT DVEAVSVVSW LFAQESLNLT TSEEAGSWDN
TLLLVELMVP NKTDSVAYID QGECSPSRYA HVVIDNRAIE DAYYQDLLVG PLPIDNATAS
YEPLDYTHTR KSAGKVRNIE ADEDLVSEWR YKIGSEIADI TMDLWGGTAM GADNDTLDIW
GIDPLYQDDG RIVRWDMFWN MPTDQFDSET LLPLGLYFKS EMTGRDSSQW KIEGWLYNNI
FYATTEEFRT AYWTPGFEKL AANVEGPWDR TDPQGEALPY DSNYPPTMIA PSGARFGVDS
EQNYVEWMGF SFYIGFSRDT GMALYDIRYK GERLLYELGL QEALAHYAGG DPVQSGTSYL
DTYYGFGPYA FELVPGYDCP EYATYLNSTF YMDETTHTHL NSICLFEFTA DYPMQRHSTS
EYVSTTKNTY FSVRSVSTVG NYDYMFTYSF FIDGSMSVEV RASGYIQSAY YTTGSDFGYQ
IQEALSGSMH DHVLNFKADF DILGTANSIQ LMKNVPVSRV FPWSDGKARN TMQLQRSFVS
NEDQGRFNWD QNSATQLLVV NTDEPNKWGE YRGYHVLPFA GAVHLTVEDS SNLVHAAHWA
EYDIQVTQQH DSEPRAAHPY NSQDVYDPPV NFAEFFNGES LDQEDLVVWL NLGMHHVPHT
GDLPNTVFTT AHTGVQFMPS NYFDMDQSRN TVNQVRINYA DGAAADVQTF GQKADSCDID
FTPVEFDLWQ YKGDVVVRKF PYDPNDPYYE TDSIV
//
