ID A0A1F8A3B1_9EURO Unreviewed; 682 AA.
AC A0A1F8A3B1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
DE Flags: Fragment;
GN ORFNames=ABOM_004904 {ECO:0000313|EMBL:OGM46216.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM46216.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM46216.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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:OGM46216.1}.
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DR EMBL; LYCR01000034; OGM46216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8A3B1; -.
DR STRING; 109264.A0A1F8A3B1; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000179179; 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.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 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:UP000179179};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 26..86
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 254..652
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 411
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 411
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGM46216.1"
SQ SEQUENCE 682 AA; 76887 MW; 4724B0854E1B002D CRC64;
WNIIRGHPLL FTYPLKYNEL GLAMFHPLDP LSPAELRKAS QTLRAYHAPT PVRFKVIDLL
EPPKASQLAY LQDQTARVQP PPRKAYTYYH KHGSTTLRKA RINLGKGIVE ADEEYPEIQG
PADIDEIERI IKVCAEHPAV QAEVERLKLP KGATIVNDPW LYGTDDANER RRLYQCYMYI
ALNDDPEANH YSVPTTFAPI FDAHTLELLE IERLPTGVGA EVESDTLPWE PVKAVEYSAR
LLGNDYFRKD VKPLHVVQPE GPSFRIDGRH VTWQKWSFHM GWNVREGPIL NNVFYDGRSL
FHRISMSEMT VPYGDPRTPY HRKQAFDLGD SGFGITSNTL TLGCDCLGLI AYFDGIRTSG
SGEPVVMKNV ICMHEVDDGV GWKHTNIRNG QASMVRNRQL VIQCTATVMN YEYILAYILD
QAGNIHIDVK ATGIVSTMPI RQKTLSPWGT VVAPGVLAVN HQHLFCLRID PALDGVKNTI
TYDDIKPVMN NPQLDPFGVA FRVHTTPISQ PGGYDLDTSQ SRTYKIINPS QINPVSGKPV
GYKLHALPSQ MLMMGPETFN YKRGHFSSKP IWVTSYRDDE FWAAGEFTNQ SREDTGLGVW
ARRNENVENE DVVLWHTFGV THVTRPEDFP VMPVEKMSVS LKPTSFFELN PSNDVPRSSQ
NMNRSTLVEH SSTAPGCGKC SL
//
