ID G3J7I0_CORMM Unreviewed; 484 AA.
AC G3J7I0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=CCM_01805 {ECO:0000313|EMBL:EGX97146.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX97146.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX97146.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX97146.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126399; EGX97146.1; -; Genomic_DNA.
DR RefSeq; XP_006667023.1; XM_006666960.1.
DR AlphaFoldDB; G3J7I0; -.
DR STRING; 983644.G3J7I0; -.
DR GeneID; 18163835; -.
DR KEGG; cmt:CCM_01805; -.
DR VEuPathDB; FungiDB:CCM_01805; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_0_3_1; -.
DR InParanoid; G3J7I0; -.
DR OMA; LWARVMH; -.
DR OrthoDB; 5471885at2759; -.
DR Proteomes; UP000001610; 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:SF14; AMINE OXIDASE; 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:UP000001610}.
FT DOMAIN 11..470
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 484 AA; 53312 MW; 82B375AA74E44570 CRC64;
MWDVVVIGAG FSGLQAAYSA KASGLSVAVV EARDRVGGKS FTIPLANGRG TADLGAAWVN
QHLQPRVWSL IERFGLAGKV VEQRLGGTAV MVTAESERIE FPFGITPHVS MPAAQDMAHR
LGSNIFYLQF TAEEQEDLVK IRDHIQAESL NPTGFRKEDD GLSLDQYVRN LGTLPKTLAM
VNLWTRVMHG LESTEESAAF FIDYCRTNHG LLSIRADDRT GGNYMRLTAG TQSIAKGLAQ
LIGADSVHLS SPVSLIEDKG SHVVVTTKNG RTFEGRKLIV SIPSALFREL DFSPPLPERL
EQVTRSTKLG HYNKALVFYH RPWWRARGFN GFMMSFQGPV CVARDTSFDD LGIYGLTCFV
NGRPGQEWAR LPPSERRRVV LEQLATVFDT GASPDARRPT EYMDQIWQHE EFSRGALAPV
PAIGHYAAFS DVYGKPAGNI HFVGTEYSRH WKGYIEGALA SGQAGAKEVL DALQKPKEAL
KSML
//
