ID A1D0G8_NEOFI Unreviewed; 661 AA.
AC A1D0G8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=NFIA_040640 {ECO:0000313|EMBL:EAW24488.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW24488.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027686; EAW24488.1; -; Genomic_DNA.
DR RefSeq; XP_001266385.1; XM_001266384.1.
DR AlphaFoldDB; A1D0G8; -.
DR STRING; 331117.A1D0G8; -.
DR EnsemblFungi; EAW24488; EAW24488; NFIA_040640.
DR GeneID; 4592497; -.
DR KEGG; nfi:NFIA_040640; -.
DR VEuPathDB; FungiDB:NFIA_040640; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_2_1; -.
DR OMA; CMHPSET; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000006702; 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:UP000006702};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 2..85
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 91..185
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 217..633
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 380
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 380
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 661 AA; 74359 MW; BEA213713FD39705 CRC64;
MLDPLSADEI TTAATLLRQH AHPTALKFNC ITLHEPLKAE LNAFLSGTGP RPARRAFSIV
LKKGTPEVSE AIVNLTTKKV ESWTSVKDVM PTLTLDDLNI IEHIASKDSR VIEACREIGI
TDMSRVYFDA WAIGIDERWG FERRLQQALP YYRSSKHDNQ YAHPLDFTVV ADTETQEILS
VDVRRVNGER TPVPLDEHNY LPQFIKDQYR PERLKAIEIT QPEGVSFKMN GNEIEWAGLK
MHVGFNYREG IVLSNVRIDD PYENRERKLF HRVSVVEMVV PYGCPKPPHH KKHAFDVGEY
GSGLMTNSLK LGCDCKGAIQ YLDAVLATST GEATVIENAI CIHEEDNGLL YKHTDFRDGN
VISARDRKLI ISQIITAANY EYAFYHTFTL DGTYKLEVKL TGMLNTYCLH PSEQAAPFGT
EIARGLDAQN HQHIFSLRVD PEIDGPSNTV VQSDAVPMAD PVGSPANPYG NGFYAKKTPL
RTALQGAADY CHETSRGWDI TNPSRLNPST RKPIAYKILN NNCPLLLAKP GSTVYKRAGF
ARHALWVLPY RDHEIFPAGQ YVCQSTGEED HPHNSTIVDW AARNESIENT DIVCYIQFGL
THFPRTEDFP IMPAEPVSVM LRASNFFQKN PALWVPPSDV VRDVSSRNAV EARELMETPR
L
//
