ID S8BT55_DACHA Unreviewed; 697 AA.
AC S8BT55;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=H072_7875 {ECO:0000313|EMBL:EPS38377.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS38377.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS38377.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS38377.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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:EPS38377.1}.
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DR EMBL; AQGS01000570; EPS38377.1; -; Genomic_DNA.
DR RefSeq; XP_011113603.1; XM_011115301.1.
DR AlphaFoldDB; S8BT55; -.
DR STRING; 1284197.S8BT55; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_2_1; -.
DR OMA; VHVGFNY; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000015100; 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.
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:UP000015100};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 23..106
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 113..214
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 240..652
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 401
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 401
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 697 AA; 77523 MW; D3D8E1BCF83E45D2 CRC64;
MGSIIDNIKQ KASTIINKFT GHHPLDPLTT SEIAKAVSII RETKGQLGYN AVTIAEPKKV
EVLAWLADPE HAPKPARQAE VVAIDKTGAI WDGIVDLASG KLLQWEKLDG VQPLITMEDL
IETDRVVKAD PKVIEQCGIL GIPASDMHKV HADPWTIGFD SRFGNTTRLQ QALMYYRPNP
DDCQYAFPLD FCPIVNTETK EVIHIDIPEV RRPLNKIPSN YNPKDIESDG TGYRTDIKPL
HVTQPQGVSF AITGREISWQ NFKVHVGFNY KEGIVLNNIT YNDKGVVRPL FYRLSLAEMV
VPYGNPEMWH YRKHAFDLGE YGGGYMTNEL ALGCDCLGEI HYLDAFFVNR AGDPVTIKNA
ICVHEEDAGI LFKHTDFRDN SVIVTRGRKL ILSHIFTAAN YEYCVYWIFH QDGTIQLEIK
LTGILNTYAM APDEDTKGWG TQVHPGVNAH NHEHLFCLRI DPQIDGQSNT IFQVDATMGP
GEVGSAENHY GNAFFAQKTK YSTVTEAIAD YNGDTSRTWD IANTNKLHPV SGKPVSYKLV
SREVPRLLIK DGGLVHKRAG FARHAVHVTK YKDGQIYPAG RHVPQSSGDP SLGLPEWIAA
NPSESIDNTD VVLWHTFGLV HFPAPEDFPV MPAEPMSLLL RPRHFFLRNP ALDVPPSFCS
TPSMVANPGL KEKVVDAADK LSRLAFGGGA RRGDCCD
//
