ID A0A066XRV4_COLSU Unreviewed; 761 AA.
AC A0A066XRV4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=CSUB01_12204 {ECO:0000313|EMBL:KDN71587.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN71587.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(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}.
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:KDN71587.1}.
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DR EMBL; JMSE01000156; KDN71587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XRV4; -.
DR STRING; 1173701.A0A066XRV4; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_3_1_1; -.
DR OMA; HYAYPIP; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000027238; 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 PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
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:UP000027238};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 253..691
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 209..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 411
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 411
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 761 AA; 84213 MW; DBAC99819EE145E8 CRC64;
MAPHPLAALS KDEFNGARDI VTRLYASDYS LFFRAIFLQE PKKAELVPFL QAEHAGVVTD
ETPRPPRRAR LQYDVIKPGS MPEYTQSVVD LKSKKEVERT VAKPTSQTAY LPDEFALFQD
ICVASQLFKD AMAEFSLPEN FAVTIDPWPY GGPDEDENIP RYMQGLVFAR DVSKGNPDSN
HYGYPIPIIP VMNFITKEIV RVDRLATGGA DDGLDPHPPS SKPKPLFANT QSPSAEYVPE
LLDMPQRADL KPINITQPEG ASFRIHADNL VEWQKWRFRL GFTPREGAVL HDLCYDGRPV
LYRLSYSELT VPYGDPRPPF HRKQAFDLGD GGFGRVANNL DLGCDCLGAI HYLDALLADT
NGNPTLAKAV VCLHEQDNGI GWKHTNFRTN RAVVTRLREF VVQCVVTLAN YEYVFAYKLD
TAGGITLETR ATGIMSVVAI DEGKTESPYG AVVAPGVLAQ NHQHVFAVRI DPAIDSYGEG
DTRVVVEESV PVPMNAATNP HGNYYEIRKR VMDRADWIDA EPRLNRVVKL ENATKRNPVS
GRNVGFKLTP SASQLMLADE ESQVSKRAKF ARHHIWVTGY RDDELWAAGE YTNQSKEEVG
GVWDMVARGD WFDDGDGDGA SGSGNMSPGE GRKSSPVIWS VFGLTHNPRV EDWPVIASIE
LVPNPDFKTR PVEIHHMNIR PADFFTANPA LDMPGSRNKA SVIVPCCEKR DGPENGTNDT
NGTNGLERGN DGVQKAALTH LQGPGPDIPA EEAGAQVRNR E
//
