ID W9WGB5_9EURO Unreviewed; 869 AA.
AC W9WGB5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=A1O7_00370 {ECO:0000313|EMBL:EXJ64035.1};
OS Cladophialophora yegresii CBS 114405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ64035.1, ECO:0000313|Proteomes:UP000019473};
RN [1] {ECO:0000313|EMBL:EXJ64035.1, ECO:0000313|Proteomes:UP000019473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ64035.1,
RC ECO:0000313|Proteomes:UP000019473};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL Submitted (MAR-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:EXJ64035.1}.
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DR EMBL; AMGW01000001; EXJ64035.1; -; Genomic_DNA.
DR RefSeq; XP_007752602.1; XM_007754412.1.
DR AlphaFoldDB; W9WGB5; -.
DR STRING; 1182544.W9WGB5; -.
DR GeneID; 19174987; -.
DR VEuPathDB; FungiDB:A1O7_00370; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_015739_0_0_1; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000019473; 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 InterPro; IPR015328; DUF1965.
DR PANTHER; PTHR10638:SF20; 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 Pfam; PF09248; DUF1965; 1.
DR PRINTS; PR00766; CUDAOXIDASE.
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:UP000019473};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 84..143
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 237..299
FT /note="DUF1965"
FT /evidence="ECO:0000259|Pfam:PF09248"
FT DOMAIN 315..732
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 743..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 469
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 469
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 869 AA; 97009 MW; BC14076D18C06126 CRC64;
MASWRSVSVS ISALVVFVVS LAYLLISASS STSALGGQQD LGPLKHPHRH FQAPAENPWA
ELDDAEASQL YLWLHENTNL FDSASDTNAL NLVELLRPNK SDVADYLDHG GPPPERWARL
SNLESKGDEA FVKEYMVGPL PPSNHTQILP LTYCHNSGRN SVRSPISDVF ALLDWALGIG
ENASDITLDL LGAKTNRHDL DDPDGLVIGS RPALIDSGRM VHWLEFFRPG MKSDGRSLLP
QGLYVKLDIP TARPETWTTG GWFYNGILYD NDTMLREAMK SPDFERLVVN EDGGWTDTED
PASVAPERDM PPPLSIQPYG PRYHLDRAEN YVSWMGFSFY VATSQATAVS LFDIRYNDTR
IIYQLGLQEA LAHYAGVEPM QSGLEFLDTF FGMGKMMFSL VPGLDCPGHA EYVDMSYHRG
GKMYTNKNAI CVFEYTSDAP LQRHTSAFSA TVSRNTYLVV RSVSTVGNYD YTIDYIFYLD
GSIEVKLRAS GYIFGAFHAE PRHSAVPPRD SSTNEYGYRI HPGVQTSMHD HVVNFRADFD
ICGTANTLVR TTVEPLKREY DWDEPEVDGP RNTMHMVHEP ITRETGLNWP KNAREMYLVT
SPSATNKWGE SRAYRILPGT GMGNPAHLTI VNSTTLGNSA AWSSADLWVL RNHPDTEPSS
AHENNYLEPL APLVDFTKMV DSEDIEGEDL VVYFNLGGHH VPTSQDVPNT LMHTSASSVV
FMPFNYFDED VSRAWRQGVR VDRRPPAREG VGSAVEKDEV KIKTKRTADA QGEENNRHRD
EDAQSEKDKR HEDEDDGVTW FGGRYTRDVL VSPQMLTPDL SHYMRERDEG EAGGWKTVRN
AVGGGLVGLF VGKERAGEEG GRGRGGMDW
//
