ID A0A3F3PZZ3_9EURO Unreviewed; 548 AA.
AC A0A3F3PZZ3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=BDQ94DRAFT_42493 {ECO:0000313|EMBL:RDH32488.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH32488.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH32488.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH32488.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|RuleBase:RU362067}.
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DR EMBL; KZ852050; RDH32488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3PZZ3; -.
DR STRING; 1341132.A0A3F3PZZ3; -.
DR OrthoDB; 1923690at2759; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF313; POLYAMINE OXIDASE 2; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..548
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017746999"
FT DOMAIN 48..489
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 548 AA; 61571 MW; B6F1C91B6D9A26A8 CRC64;
MHTIPITVSL YAFLATTFLF SCSAYVAQAP LSDDKCTETT VAILGGGMAG IAAAQALSNA
SIDDFIILEY RDTLGGRVWH TDFGKDKQGK PYVIELGANW LQGLGSEAIE NPVWALAKKY
SLKNTYSNYS SIRTYNETGY TDYRYLLDEY AQAYHIAARD AGRILTQNLQ DQTARTGLAL
AGWRPRKNDM AAQAVEWWSW DWEDAHTPET SSLVFGIAGE NLTFNQFGKA NHLVLDPRGY
STIIQNEALG FLPNPSDGRL RLNTRVTRIE YSPRGVTIHT TNDNNKNSNT CIRAAYAICT
FSLGVLQNKA VTFDPPLPSW KQTAIEKFNM GTYTKIFMQF PETFWPTDTQ FFLYASPTTR
GYYPVFQSLS TENFLPESNI LFATVVDEQA YRVERQSLTQ TKDQILDVLR EMFPDKHIPE
PTAFTYPRWT NEPWVYGSYS NWPAGTTLEM HQNLRANTGR LWFAGEATSA AYFGFLHGAW
YEGRDAGENV AALLQGRCVE DVSTASTASG KEEKEEACGE RVFYEQLNGT TPLDAYSRLN
GWPAVSYY
//
