ID A0A0A2VT07_BEABA Unreviewed; 709 AA.
AC A0A0A2VT07;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=BBAD15_g5196 {ECO:0000313|EMBL:KGQ09497.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ09497.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ09497.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ09497.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ09497.1}.
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DR EMBL; ANFO01000440; KGQ09497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VT07; -.
DR STRING; 1245745.A0A0A2VT07; -.
DR EnsemblFungi; BB8028_0002g11350.1; BB8028_0002g11350.1; BB8028_0002g11350.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_2_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0052595; F:aliphatic amine oxidase activity; IEA:RHEA.
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; IPR015802; Cu_amine_oxidase_N3.
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 Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 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:UP000030106};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 37..122
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 128..222
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 255..670
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 417
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 417
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 709 AA; 79573 MW; E927BAF509E0FDE9 CRC64;
MANPALQPDL DLIAGYEVYP EQTYDPKTAA SLRHQTHPLD QLSMQEISHA VKMIRDKASP
AEVKFNCVTL REPRKAEYAA FKAGSGPRPE RKAFAIIIQR GSNSCAEVVV NLTNSTIESW
KPVSEVAPTL TLEDLDVMER ISRKDPRVIR ACEEIGITDM SKVYLDGWAV GFDDRWDFSR
RLQQGLAYYR HSPNDNQYAH PLDFCVVADT ETEEVLSVDI RYVNGERTLP PLDQHNFLPE
FIEQGYNTTK LKPLDITQPE GVSFQIRGNE LSWAGYKMHI GFNYREGIVI SDVRIDDPYE
ARERTLFNRI SVVEMVVPYG NPDPPHHRKH AFDVGEYGTG LMTNSLKLGC DCKGAIHYMD
GIMSTSSGLP AVLKNAICIH EEDNGILYKH MDYRDASTVL ARDRKLIISQ IITAANYEYA
FYHTFTLDGT YKLEIKLTGI LNSYCLHPSE TAAPYGTEVA RGITAHNHQH IFSLRVDPEI
DGTNNTVIQN DAVTSEAPLG SAENPYGNGF YCKKTPLRTA KQGAVEYKHE TSRNWDIVNP
NVINEVCHKP VGYKIVNTQC PALLAKPGSM VYKRAGFATK SLFVLPYKDY ELFPAGDYVC
QSTGEPGHPD SSVITDWVER DENIENTDIV CYVQFGLTHF PRCEDFPLMP AEPVMIMIRA
SNFFVRNPAL WVPPSTVVKD LSSRTAFLTT GNESNGSCCV SKKTPDSHL
//
