ID A0A084R0E3_STAC4 Unreviewed; 756 AA.
AC A0A084R0E3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=S40285_05932 {ECO:0000313|EMBL:KFA69678.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA69678.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA69678.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA69678.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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; KL659381; KFA69678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084R0E3; -.
DR STRING; 1283841.A0A084R0E3; -.
DR HOGENOM; CLU_011500_3_1_1; -.
DR InParanoid; A0A084R0E3; -.
DR OMA; HYAYPIP; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000028524; 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; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF94; PRIMARY 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.
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:UP000028524};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 5..100
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 251..675
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 610..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 409
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 409
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 756 AA; 83418 MW; 5FD39658AD454C39 CRC64;
MAVPHPLAQL SPDELVKARD IIAKLHSSAE SLFFRAAYLQ EPKKSDLVPF LELEHSGQLT
DGAKRPPRQA RVEYDVIGAQ HHEHYRAVVD LGTGQLVSKD VAEQKAYPYY TPGEFAQFQD
ACVASELFRD AMSEFTLPEG YDVSIDPWPY GGPDDTEDPD RYMQGLVFAV DSTKQNPDSN
HYAYPIPIIP VMDWVKKEII RVDRLATGGS TDGMAPEPKQ DSPRKLFQGN QAAEYVPELL
DTPLREGLKP INITQPEGAS FSIHGDGLVE WQNWRFRLGF TPREGAVLHD VCYENRPIVY
RLSYSELTVP YADPRPPFHR KQAFDFGDGG IGRAANNLEL GCDCLGAIHY VDAYLPAPDG
SPTSAKSVIC LHEQDNGILW KHTNFRTNRA VVTRMRELVV QFIATLANYE YVFAFKLDLA
GNITIETRAT GIVSVVSIDE GKTSKYGNVV APGILAQNHQ HIFAVRIDPA IDSYASDGTQ
VVVEESVGQP ITKEANPYGN YYEIQRQNVE HATWIDAEPR LNRLLKLESS VKKNSISGKN
VGYKLVAPAT QMLLANDDSV LAKRARYAQH NTWVTGYRDG ELWAAGEYTN QSRAEKGGVT
DMVKRGDWFM GDGKPTNGTS NGDASHGDGQ RSSPVVWSVF GLTHNPRVED WPVMPVEIYQ
IHLRPADFFT RNPALDVPST KNQASVLVPC CGGDAAATNG AEQKGISASE QQNPLAHLQG
TGPDIKAETA GASEADDGKA ESKLSKAFTD LFKRDK
//
