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Database: UniProt
Entry: E3QIU0_COLGM
LinkDB: E3QIU0_COLGM
Original site: E3QIU0_COLGM 
ID   E3QIU0_COLGM            Unreviewed;       614 AA.
AC   E3QIU0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN   ORFNames=GLRG_05922 {ECO:0000313|EMBL:EFQ30778.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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}.
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DR   EMBL; GG697351; EFQ30778.1; -; Genomic_DNA.
DR   RefSeq; XP_008094798.1; XM_008096607.1.
DR   AlphaFoldDB; E3QIU0; -.
DR   STRING; 645133.E3QIU0; -.
DR   EnsemblFungi; EFQ30778; EFQ30778; GLRG_05922.
DR   GeneID; 24411287; -.
DR   VEuPathDB; FungiDB:GLRG_05922; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   HOGENOM; CLU_004498_0_3_1; -.
DR   OrthoDB; 5471885at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.1330.40; RutC-like; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   InterPro; IPR035959; RutC-like_sf.
DR   InterPro; IPR006175; YjgF/YER057c/UK114.
DR   PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR   PANTHER; PTHR43563:SF14; AMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF01042; Ribonuc_L-PSP; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55298; YjgF-like; 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:UP000008782}.
FT   DOMAIN          157..602
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   614 AA;  66123 MW;  E1C76847A9EACDCF CRC64;
     MPPKVRALDL DNTSTAYYAS ATVAPSGARL VHVSGQPGNT KDDVVPDDYE SQIHLALLNL
     RKIIIVAGAS VKDIVKLTLL IVDYDSSARK HTRHIQRFLG GHRPAITLIP VSKLAVSSWL
     FEIDAVLAVP ETPAPARGLA LPDADESVDV VIIGAGLAGL SAARDVLKSG LSCVVLEARD
     RVGGKTWSEP LQDGQPGVVD LGAAWINDTN QSRVYALAKE YGAELIEQNT NGDVVLQDFD
     GKCSPFPYGE LPFFDEATRK ALAGIRDMVE ADCQAVDTWK PKDTSLDSLT FAAYLRLRGA
     DDVAMATANV WTCAMLGQEA TDISALYFLN YCKSGGGLLQ MRSDRKDGGQ YLRVRQGTQV
     FSKGLASSLP EGVVRLSRPV RAVVRDDHPG GGRYAVKVQT DEGVLAARKV ITTIPGPALK
     NISFRPALPL PKQAWIESLS YGYYTKAMMQ FESPFWVERG FCGLAQSFVG PASVIRDTSV
     PADSKHVLTC FMAGDRGRAW AALDAPAREK SLLAQLAQLF GCEDIQSRFV RMSTYEWVKD
     EWSGWGCPCT SLAPGVLDTL GGDSLRKSCG DLHFAGTETA GEWKGYMEGA VRSGERAAAE
     VIEALTSTSG ASRL
//
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