ID A0A066X8L1_COLSU Unreviewed; 461 AA.
AC A0A066X8L1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=CSUB01_10406 {ECO:0000313|EMBL:KDN62076.1};
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:KDN62076.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000205};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}.
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:KDN62076.1}.
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DR EMBL; JMSE01001359; KDN62076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066X8L1; -.
DR STRING; 1173701.A0A066X8L1; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_0_4_1; -.
DR OMA; YNTGNCT; -.
DR OrthoDB; 5471885at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF1; FLAVIN-CONTAINING MONOAMINE OXIDASE B-RELATED; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT DOMAIN 22..454
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 461 AA; 51144 MW; F3AAC72CAB35CDDF CRC64;
MDEATTDITP MYDCVVIGAG YSGLAAARLL KDSGKHILVL EALDRVGGRA KTIPVGDGEY
WDVGASFLGD QQDLMYALAT EFGVPLHTTP TNGKIVLAYR GKAREYSGLI PPMRPWEVID
MGMFVRRFEK LCESVNLEKP WLTPNADELD RITVREWLMK GAWTQATIDM GNLAFETTIG
QNTSCISMLH AMFFFKGVIN LTSALSSENG AQKHFIQGGG QAIAKKLMDY LGDGTVHLEE
PVHKISYSKS VAIIQTEQAT YRTRRIISAI PPGNVLKIEF EPRLPMEKES LLQNMPMGSF
TKVYATYKRP FWRERGLTGE STNPDGFVSV TFDATPPSGS PAKLMGFVAS TKSREFMSFS
KDKRRHVALG GFAAAFGQEA LDSEDFFCHN MMEENWSFGC PMATPAPGMW SLFGEWMRKP
VGAIHWAGTE TSTKHYGYME GAVFAGQRSA REVLGELKWK I
//
