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
//